During the colonization of land, abiotic and biotic challenges induced strong adaptations in plants, including changes of their cell walls. Up to now, cell walls of spore-bearing plants have been only sparsely investigated. As ferns are the sister group to seed plants, studying their cell walls is key to understanding the evolutionary development of the cell wall in the tracheophyte lineage. Beside polysaccharides, especially arabinogalactan-proteins (AGPs) are important cell wall components involved in structural but also signalling functions. We chose a member of the eusporangiate ferns, Psilotum nudum, to characterize and immunolocalize AGPs. Biochemical analyses identified special structural features of P. nudum AGPs in comparison to A. thaliana AGPs, including lower amounts of 1,6-linkage in the galactan core. With regard to the arabinose (Ara) residues, A. thaliana AGP was dominated by terminal furanosidic Ara, followed by 1,5-Ara, whereas in P. nudum AGPs, 1,3-Ara, terminal furanosidic Ara and terminal pyranosidic Ara occurred in comparable amounts. Terminal pyranosidic rhamnose was only found in the fern AGP. Immunofluorescence analysis using JIM13 antibody detected AGPs in all tissues of the P. nudum stem with the exception of the mature protoxylem. Localization was observed along the plasma membrane as well as tonoplast.
在陆地的殖民过程中，非生物和生物的挑战引起了植物的强烈适应，包括细胞壁的变化。到目前为止，对孢子植物细胞壁的研究还很少。蕨类植物是种子植物的姐妹类群，研究蕨类植物的细胞壁是了解管生植物细胞壁进化发育的关键。除了多糖，特别是阿拉伯半乳糖蛋白（AGPs）是细胞壁的重要成分，参与结构和信号功能。我们选择了一种蕨类植物裸蕨（Psilotum nudum）来表征和免疫定位agp。生化分析发现，与拟南芥AGPs相比，裸p.n umum AGPs具有特殊的结构特征，包括在半乳糖核心中较少的1,6-连锁。在阿拉伯糖（Ara）残基方面，拟南芥AGP以末端呋喃基Ara为主，其次是1,5-Ara，而在拟南芥AGP中，1,3-Ara、末端呋喃基Ara和末端吡喃基Ara的数量相当。末端吡喃鼠李糖仅存在于蕨类植物中。利用JIM13抗体进行免疫荧光分析，除成熟的原木质部外，在裸豆茎的所有组织中均检测到AGPs。沿质膜和张力质体观察到定位。
{"title":"Arabinogalactan-proteins of the eusporangiate fern Psilotum nudum show atypical structural features compared to other ferns","authors":"Kim-Kristine Mueller , Lukas Pfeifer , Urska Repnik , Marc Bramkamp , Birgit Classen","doi":"10.1016/j.tcsw.2025.100157","DOIUrl":"10.1016/j.tcsw.2025.100157","url":null,"abstract":"<div><div>During the colonization of land, abiotic and biotic challenges induced strong adaptations in plants, including changes of their cell walls. Up to now, cell walls of spore-bearing plants have been only sparsely investigated. As ferns are the sister group to seed plants, studying their cell walls is key to understanding the evolutionary development of the cell wall in the tracheophyte lineage. Beside polysaccharides, especially arabinogalactan-proteins (AGPs) are important cell wall components involved in structural but also signalling functions. We chose a member of the eusporangiate ferns, <em>Psilotum nudum</em>, to characterize and immunolocalize AGPs. Biochemical analyses identified special structural features of <em>P. nudum</em> AGPs in comparison to <em>A. thaliana</em> AGPs, including lower amounts of 1,6-linkage in the galactan core. With regard to the arabinose (Ara) residues, <em>A. thaliana</em> AGP was dominated by terminal furanosidic Ara, followed by 1,5-Ara, whereas in <em>P. nudum</em> AGPs, 1,3-Ara, terminal furanosidic Ara and terminal pyranosidic Ara occurred in comparable amounts. Terminal pyranosidic rhamnose was only found in the fern AGP. Immunofluorescence analysis using JIM13 antibody detected AGPs in all tissues of the <em>P. nudum</em> stem with the exception of the mature protoxylem. Localization was observed along the plasma membrane as well as tonoplast.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100157"},"PeriodicalIF":6.2,"publicationDate":"2025-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145361022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Trichoderma harzianum is a saprophyte and a mycoparasite and is also capable of forming symbiotic connections with plants. This fungus interacts with the (a)biotic environment through its cell wall and as a mycoparasite secretes enzymes that degrade the cell wall polymers of its target fungi. The organization of the T. harzianum cell wall is not well known. We used solid-state NMR and Fourier transform infrared spectroscopy to probe the molecular composition and architecture of the T. harzianum cell wall at the atomic level. Our results revealed that the inner core of the T. harzianum rigid cell wall phase is largely composed of chitin, which is complemented with a more mobile cell wall layer that contains β-(1,3)-glucan. The outer dynamic phase of the cell wall is mainly composed of α- and β-glucans, arabinan, mannan and proteins. The relative abundance of both rigid and dynamic cell wall components changed when T. harzianum was grown on isolated fungal cell wall material instead of glucose. Our results suggest that T. harzianum forms a cell wall that is chemically distinct from other fungal species to prevent harmful self-digestion by its secreted lytic enzymes that do degrade the cell wall of target fungi.
{"title":"Solid-state NMR spectroscopy reveals unique properties of Trichoderma harzianum cell wall components","authors":"A.A. Safeer , F.E.L. Kleijburg , H.A.B. Wösten , M. Baldus","doi":"10.1016/j.tcsw.2025.100156","DOIUrl":"10.1016/j.tcsw.2025.100156","url":null,"abstract":"<div><div><em>Trichoderma harzianum</em> is a saprophyte and a mycoparasite and is also capable of forming symbiotic connections with plants. This fungus interacts with the (a)biotic environment through its cell wall and as a mycoparasite secretes enzymes that degrade the cell wall polymers of its target fungi. The organization of the <em>T</em>. <em>harzianum</em> cell wall is not well known. We used solid-state NMR and Fourier transform infrared spectroscopy to probe the molecular composition and architecture of the <em>T</em>. <em>harzianum</em> cell wall at the atomic level. Our results revealed that the inner core of the <em>T. harzianum</em> rigid cell wall phase is largely composed of chitin, which is complemented with a more mobile cell wall layer that contains β-(1,3)-glucan. The outer dynamic phase of the cell wall is mainly composed of α- and β-glucans, arabinan, mannan and proteins. The relative abundance of both rigid and dynamic cell wall components changed when <em>T</em>. <em>harzianum</em> was grown on isolated fungal cell wall material instead of glucose. Our results suggest that <em>T. harzianum</em> forms a cell wall that is chemically distinct from other fungal species to prevent harmful self-digestion by its secreted lytic enzymes that do degrade the cell wall of target fungi.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100156"},"PeriodicalIF":6.2,"publicationDate":"2025-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145324526","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-29DOI: 10.1016/j.tcsw.2025.100155
Shogo Yoshimoto , Jun Sasahara , Atsuo Suzuki , Junichi Kanie , Kotaro Koiwai , Andrei N. Lupas , Katsutoshi Hori
Trimeric autotransporter adhesins (TAAs) are outer membrane (OM) proteins that are widely distributed in gram-negative bacteria and are involved primarily in adhesion to biotic and abiotic surfaces, cell agglutination, and biofilm formation. TAAs consist of a passenger domain, which is secreted onto the cell surface, and a transmembrane domain, which forms a pore in the OM to secrete and anchor the passenger domain. Because the interactions between TAAs and chaperones or dedicated auxiliary proteins during secretion are short-lived, TAAs are thought to reside on the OM without forming complexes with other proteins after secretion. In this study, we aimed to clarify the interactions between an Acinetobacter TAA, AtaA, and a peptidoglycan (PG)-binding periplasmic protein, TpgA. Pull-down assays using recombinant proteins identified the interacting domains. X-ray crystallography at 2.6 Å resolution revealed an A3B3 heterohexameric complex structure composed of the N-terminal domain of TpgA and the transmembrane domain of AtaA. TpgA-N consists of two short α helices and three antiparallel β strands, yielding an ααβββ topology similar to BamE. However, the regions corresponding to BamE interfaces with BamA and BamD differ in TpgA-N. All-atom molecular dynamics simulations and mutational assays revealed that both electrostatic and hydrophobic interactions contribute to stable complex formation. Bioinformatic analyses indicate that the TAA-TpgA complex occurs in a wide range of species. These findings will contribute to a better understanding of TAAs and the cell envelope.
{"title":"Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein","authors":"Shogo Yoshimoto , Jun Sasahara , Atsuo Suzuki , Junichi Kanie , Kotaro Koiwai , Andrei N. Lupas , Katsutoshi Hori","doi":"10.1016/j.tcsw.2025.100155","DOIUrl":"10.1016/j.tcsw.2025.100155","url":null,"abstract":"<div><div>Trimeric autotransporter adhesins (TAAs) are outer membrane (OM) proteins that are widely distributed in gram-negative bacteria and are involved primarily in adhesion to biotic and abiotic surfaces, cell agglutination, and biofilm formation. TAAs consist of a passenger domain, which is secreted onto the cell surface, and a transmembrane domain, which forms a pore in the OM to secrete and anchor the passenger domain. Because the interactions between TAAs and chaperones or dedicated auxiliary proteins during secretion are short-lived, TAAs are thought to reside on the OM without forming complexes with other proteins after secretion. In this study, we aimed to clarify the interactions between an <em>Acinetobacter</em> TAA, AtaA, and a peptidoglycan (PG)-binding periplasmic protein, TpgA. Pull-down assays using recombinant proteins identified the interacting domains. X-ray crystallography at 2.6 Å resolution revealed an A3B3 heterohexameric complex structure composed of the N-terminal domain of TpgA and the transmembrane domain of AtaA. TpgA-N consists of two short α helices and three antiparallel β strands, yielding an ααβββ topology similar to BamE. However, the regions corresponding to BamE interfaces with BamA and BamD differ in TpgA-N. All-atom molecular dynamics simulations and mutational assays revealed that both electrostatic and hydrophobic interactions contribute to stable complex formation. Bioinformatic analyses indicate that the TAA-TpgA complex occurs in a wide range of species. These findings will contribute to a better understanding of TAAs and the cell envelope.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100155"},"PeriodicalIF":6.2,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-22DOI: 10.1016/j.tcsw.2025.100154
Deeksha Pandey , Isha Gupta , Dinesh Gupta
Background
AmpC β-lactamases (blaAmpC) are essential drivers of antimicrobial resistance (AMR) in ESKAPE pathogens, bacteria that cause hospital-acquired infections. Understanding AmpC enzymes is essential for uncovering resistance mechanisms and guiding antimicrobial strategies. We analyzed blaAmpC presence, genomic location, copy number, sequence variability, and evolutionary traits in ESKAPE pathogens.
Results
We identified 1790 AmpC enzymes in 4713 complete genomes, classified into nine enzyme groups. Consistent with known taxonomic profiles, no class C β-lactamases were detected in Gram-positive bacteria (Staphylococcus aureus and Enterococcus faecium). Acinetobacter baumannii exhibited the highest occurrence of class C β-lactamases, with Enterobacter spp. showing the second highest prevalence, followed by Pseudomonas aeruginosa and Klebsiella pneumoniae. The largest enzyme group, ADC was restricted to A. baumannii; similarly, ACC, ACT, CMH, and MIR to Enterobacter spp.; and PDC and PIB to P. aeruginosa. Phylogenetic analysis showed divergence among some groups and closer evolutionary relationships in others. Functional Motif analysis revealed conserved catalytic residues across all groups except PIB. Instead of the canonical YXN and KTG motifs, PIB contains YST and AQG variants, respectively. Because of these variations, PIB's ability to bind cephalosporins decreases while enhancing their activity against carbapenems.
Conclusions
We identified 1790 AmpC enzymes in nine distinct groups across ESKAPE pathogens, with species-specific distribution patterns and notable absence in Gram-positive bacteria. The PIB enzyme group demonstrated unique motif variants (YST/AQG) conferring carbapenem resistance, while other groups maintained conserved catalytic motifs. Phylogenetic analysis revealed evolutionary divergence and horizontal gene transfer potential, emphasizing the need for targeted therapeutic approaches against AmpC-mediated resistance.
{"title":"AmpC β-lactamases: A key to antibiotic resistance in ESKAPE pathogens","authors":"Deeksha Pandey , Isha Gupta , Dinesh Gupta","doi":"10.1016/j.tcsw.2025.100154","DOIUrl":"10.1016/j.tcsw.2025.100154","url":null,"abstract":"<div><h3>Background</h3><div>AmpC β-lactamases (<em>blaAmpC</em>) are essential drivers of antimicrobial resistance (AMR) in ESKAPE pathogens, bacteria that cause hospital-acquired infections. Understanding AmpC enzymes is essential for uncovering resistance mechanisms and guiding antimicrobial strategies. We analyzed <em>blaAmpC</em> presence, genomic location, copy number, sequence variability, and evolutionary traits in ESKAPE pathogens.</div></div><div><h3>Results</h3><div>We identified 1790 AmpC enzymes in 4713 complete genomes, classified into nine enzyme groups. Consistent with known taxonomic profiles, no class C β-lactamases were detected in Gram-positive bacteria (<em>Staphylococcus aureus</em> and <em>Enterococcus faecium</em>). <em>Acinetobacter baumannii</em> exhibited the highest occurrence of class C β-lactamases, with <em>Enterobacter</em> spp. showing the second highest prevalence, followed by <em>Pseudomonas aeruginosa</em> and <em>Klebsiella pneumoniae</em>. The largest enzyme group, ADC was restricted to <em>A. baumannii</em>; similarly, ACC, ACT, CMH, and MIR to <em>Enterobacter</em> spp.; and PDC and PIB to <em>P. aeruginosa.</em> Phylogenetic analysis showed divergence among some groups and closer evolutionary relationships in others. Functional Motif analysis revealed conserved catalytic residues across all groups except PIB. Instead of the canonical YXN and KTG motifs, PIB contains YST and AQG variants, respectively. Because of these variations, PIB's ability to bind cephalosporins decreases while enhancing their activity against carbapenems.</div></div><div><h3>Conclusions</h3><div>We identified 1790 AmpC enzymes in nine distinct groups across ESKAPE pathogens, with species-specific distribution patterns and notable absence in Gram-positive bacteria. The PIB enzyme group demonstrated unique motif variants (YST/AQG) conferring carbapenem resistance, while other groups maintained conserved catalytic motifs. Phylogenetic analysis revealed evolutionary divergence and horizontal gene transfer potential, emphasizing the need for targeted therapeutic approaches against AmpC-mediated resistance.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100154"},"PeriodicalIF":6.2,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219466","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-19DOI: 10.1016/j.tcsw.2025.100153
Bianca A.G. Sena , Marlon D.M. Santos , Cassia M. Souza , Amanda C. Camillo-Andrade , Haroldo C. de Oliveira , Flavia C.G. Dos Reis , Rafael F. Castelli , Diogo Kuczera , Henrique R.M. Antoniolli , Hellen G.G. Santos , Charley C. Staats , Guilherme L. Sassaki , Paulo C. Carvalho , Marcio L. Rodrigues
Pathogenic determinants in the Cryptococcus genus have been extensively studied, often using standard laboratory isolates. Here, we analyzed the virulence of ten Cryptococcus isolates from diverse sources, species, and genotypes. These isolates exhibited marked differences in their ability to colonize and kill the invertebrate host Galleria mellonella, as well as in their interactions with hemocytes. Capsule formation also varied widely among isolates, with no clear correlation between virulence in G. mellonella and source of isolation, species, fungal burden, capsule size, or interaction with larval hemocytes. To further investigate the basis of this pathogenic diversity, we selected two hypervirulent isolates (C. deuterogattii and C. neoformans) and two hypovirulent isolates (C. gattii and C. neoformans) for in-depth analysis. Differences in the induction of antimicrobial peptides during infection did not account for the observed variation in virulence. Genomic analysis of capsule-related genes, scanning electron microscopy of capsule morphology in vitro and in vivo, and nuclear magnetic resonance of the major capsular polysaccharide all revealed high variability among isolates, but none of these features correlated with virulence. Proteomic profiling of cellular extracts showed that virulent strains were enriched in proteins associated with oxidative processes. Supplementation with an antioxidant during infection increased the virulence of hypovirulent isolates in G. mellonella. These results reveal a high pathogenic diversity in Cryptococcus that goes beyond its classical virulence factors.
{"title":"Pathogenic diversity of Cryptococcus in Galleria mellonella extends beyond classical virulence factors","authors":"Bianca A.G. Sena , Marlon D.M. Santos , Cassia M. Souza , Amanda C. Camillo-Andrade , Haroldo C. de Oliveira , Flavia C.G. Dos Reis , Rafael F. Castelli , Diogo Kuczera , Henrique R.M. Antoniolli , Hellen G.G. Santos , Charley C. Staats , Guilherme L. Sassaki , Paulo C. Carvalho , Marcio L. Rodrigues","doi":"10.1016/j.tcsw.2025.100153","DOIUrl":"10.1016/j.tcsw.2025.100153","url":null,"abstract":"<div><div>Pathogenic determinants in the <em>Cryptococcus</em> genus have been extensively studied, often using standard laboratory isolates. Here, we analyzed the virulence of ten <em>Cryptococcus</em> isolates from diverse sources, species, and genotypes. These isolates exhibited marked differences in their ability to colonize and kill the invertebrate host <em>Galleria mellonella</em>, as well as in their interactions with hemocytes. Capsule formation also varied widely among isolates, with no clear correlation between virulence in <em>G. mellonella</em> and source of isolation, species, fungal burden, capsule size, or interaction with larval hemocytes. To further investigate the basis of this pathogenic diversity, we selected two hypervirulent isolates (<em>C. deuterogattii</em> and <em>C. neoformans</em>) and two hypovirulent isolates (<em>C. gattii</em> and <em>C. neoformans</em>) for in-depth analysis. Differences in the induction of antimicrobial peptides during infection did not account for the observed variation in virulence. Genomic analysis of capsule-related genes, scanning electron microscopy of capsule morphology in vitro and in vivo, and nuclear magnetic resonance of the major capsular polysaccharide all revealed high variability among isolates, but none of these features correlated with virulence. Proteomic profiling of cellular extracts showed that virulent strains were enriched in proteins associated with oxidative processes. Supplementation with an antioxidant during infection increased the virulence of hypovirulent isolates in <em>G. mellonella</em>. These results reveal a high pathogenic diversity in <em>Cryptococcus</em> that goes beyond its classical virulence factors.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100153"},"PeriodicalIF":6.2,"publicationDate":"2025-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145157505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-12DOI: 10.1016/j.tcsw.2025.100152
Daniel A. Salgado-Bautista, Meritxell Riquelme
Extracellular vesicles (EVs) are nanosized, lipid bilayer-enclosed particles secreted by all living organisms. While EV research has primarily focused on mammalian systems, fungal EVs are gaining attention for their biological significance. Here, we investigated how growth conditions influence the protein cargo of EVs produced by Neurospora crassa, a non-pathogenic filamentous fungus and well-established model organism. EVs were isolated from cultures grown on glucose for 16 h (G16) and on sucrose for 16 (S16) and 24 h (S24). Dynamic light scattering (DLS) revealed similar size distributions for S16 and S24 EVs (24–165 nm), whereas G16 EVs exhibited a broader range (32–825 nm). Across all conditions, particles <50 nm were detected, potentially corresponding to mitochondrial-derived vesicles (MDVs) or exomeres, EV subtypes described in mammalian systems. Proteomic profiling identified 682 proteins in G16, 668 in S16, and a reduced set of 367 proteins in S24. Regardless of condition, EVs were enriched in proteins related to cell wall remodeling, protein synthesis, and carbohydrate metabolism. A high proportion of intracellular proteins confirms that fungal EVs participate in unconventional secretion. In addition, the detection of proteins involved in vesicle biogenesis and trafficking suggests that EV formation may also involve the classical secretory pathway. These findings demonstrate that EV composition and biogenesis in N. crassa are modulated by growth conditions and highlight the importance of physiological context in fungal EV research. Notably, the data reveal a diversity of EV types, including forms potentially unrelated to exosomes, expanding our understanding of fungal EV complexity.
细胞外囊泡（EVs）是由所有生物分泌的纳米级脂质双层封闭颗粒。虽然EV研究主要集中在哺乳动物系统，但真菌EV因其生物学意义而受到关注。在这里，我们研究了生长条件如何影响粗神经孢子菌（一种非致病性丝状真菌和成熟的模式生物）产生的电动汽车的蛋白质货物。从葡萄糖培养16 h （G16）、蔗糖培养16 h （S16）和24 h （S24）中分离出ev。S16和S24电动汽车的动态光散射（DLS）尺寸分布相似（24 ~ 165 nm），而G16电动汽车的动态光散射范围更广（32 ~ 825 nm）。在所有条件下，检测到50 nm的颗粒，可能对应于线粒体衍生囊泡（mdv）或外显子，哺乳动物系统中描述的EV亚型。蛋白质组学分析在G16中鉴定了682个蛋白，在S16中鉴定了668个蛋白，在S24中鉴定了367个蛋白。无论在何种情况下，EVs都富含与细胞壁重塑、蛋白质合成和碳水化合物代谢相关的蛋白质。高比例的细胞内蛋白证实真菌EVs参与非常规分泌。此外，对参与囊泡生物发生和运输的蛋白质的检测表明，EV的形成也可能涉及经典的分泌途径。这些研究结果表明，生长条件可调节草单胞菌的组成和生物发生，并强调了生理环境在真菌EV研究中的重要性。值得注意的是，这些数据揭示了EV类型的多样性，包括可能与外泌体无关的形式，扩大了我们对真菌EV复杂性的理解。
{"title":"Growth conditions shape the proteome and diversity of Neurospora crassa extracellular vesicles","authors":"Daniel A. Salgado-Bautista, Meritxell Riquelme","doi":"10.1016/j.tcsw.2025.100152","DOIUrl":"10.1016/j.tcsw.2025.100152","url":null,"abstract":"<div><div>Extracellular vesicles (EVs) are nanosized, lipid bilayer-enclosed particles secreted by all living organisms. While EV research has primarily focused on mammalian systems, fungal EVs are gaining attention for their biological significance. Here, we investigated how growth conditions influence the protein cargo of EVs produced by <em>Neurospora crassa</em>, a non-pathogenic filamentous fungus and well-established model organism. EVs were isolated from cultures grown on glucose for 16 h (G16) and on sucrose for 16 (S16) and 24 h (S24). Dynamic light scattering (DLS) revealed similar size distributions for S16 and S24 EVs (24–165 nm), whereas G16 EVs exhibited a broader range (32–825 nm). Across all conditions, particles <50 nm were detected, potentially corresponding to mitochondrial-derived vesicles (MDVs) or exomeres, EV subtypes described in mammalian systems. Proteomic profiling identified 682 proteins in G16, 668 in S16, and a reduced set of 367 proteins in S24. Regardless of condition, EVs were enriched in proteins related to cell wall remodeling, protein synthesis, and carbohydrate metabolism. A high proportion of intracellular proteins confirms that fungal EVs participate in unconventional secretion. In addition, the detection of proteins involved in vesicle biogenesis and trafficking suggests that EV formation may also involve the classical secretory pathway. These findings demonstrate that EV composition and biogenesis in <em>N. crassa</em> are modulated by growth conditions and highlight the importance of physiological context in fungal EV research. Notably, the data reveal a diversity of EV types, including forms potentially unrelated to exosomes, expanding our understanding of fungal EV complexity.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100152"},"PeriodicalIF":6.2,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145060082","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-26DOI: 10.1016/j.tcsw.2025.100151
Chengxuan Yu, Xiaoli Xu, Jia Shi, Wenqing Chu, Na Jiang, Jianqiang Li, Laixin Luo
CmWag31 is a member of the DivIVA family of proteins in Clavibacter michiganensis. The DivIVA family have been demonstrated to play a key role in the synthesis of cell wall peptidoglycan and cell division in most bacterial species. It has been previously confirmed that the pbpC (penicillin-binding protein C) deletion mutants affect bacterial division and cell wall synthesis. Based on the confirmation of the interaction between CmWag31 and CmPBPC, the present study conducted a systemic analysis on their localization characteristics. The results indicated that CmWag31 exhibited the capacity to interact with the transglycosylase (TG) and transpeptidase (TP) domain of CmPBPC, while CmPBPC only interacted with the NTD region of CmWag31. Co-localization analysis showed that CmWag31 co-localized with CmPBPC at the bacterial growth tips of Clavibacter michiganensis and Escherichia coli. The mutation of R19A, R19C, A99T, and A102T of CmWag31 resulted in abnormal localization in Escherichia coli. In the case of C. michiganensis, the CmWag31A102T protein exhibited a diffuse localization, which is a departure from the polar localization of its wild type. The co-localization of the CmWag31A102T mutation with CmPBPC exhibited discrepancies between C. michiganensis and E. coli. The diffused localization of CmWag31A102T can be restored by overexpression of CmPBPC in C. michiganensis, yet this restoration is not observed in E. coli. This result indicates that CmPBPC from C. michiganensis may not fully excute their function in E. coli due to species-specific differences.
{"title":"Localization characteristics of cell wall synthesis protein Wag31 and penicillin binding protein C in Clavibacter michiganensis","authors":"Chengxuan Yu, Xiaoli Xu, Jia Shi, Wenqing Chu, Na Jiang, Jianqiang Li, Laixin Luo","doi":"10.1016/j.tcsw.2025.100151","DOIUrl":"10.1016/j.tcsw.2025.100151","url":null,"abstract":"<div><div>CmWag31 is a member of the DivIVA family of proteins in <em>Clavibacter michiganensis</em>. The DivIVA family have been demonstrated to play a key role in the synthesis of cell wall peptidoglycan and cell division in most bacterial species. It has been previously confirmed that the <em>pbp</em>C (penicillin-binding protein C) deletion mutants affect bacterial division and cell wall synthesis. Based on the confirmation of the interaction between CmWag31 and CmPBPC, the present study conducted a systemic analysis on their localization characteristics. The results indicated that CmWag31 exhibited the capacity to interact with the transglycosylase (TG) and transpeptidase (TP) domain of CmPBPC, while CmPBPC only interacted with the NTD region of CmWag31. Co-localization analysis showed that CmWag31 co-localized with CmPBPC at the bacterial growth tips of <em>Clavibacter michiganensis</em> and <em>Escherichia coli</em>. The mutation of R19A, R19C, A99T, and A102T of CmWag31 resulted in abnormal localization in <em>Escherichia coli</em>. In the case of <em>C. michiganensis,</em> the CmWag31<sup>A102T</sup> protein exhibited a diffuse localization, which is a departure from the polar localization of its wild type. The co-localization of the CmWag31<sup>A102T</sup> mutation with CmPBPC exhibited discrepancies between <em>C. michiganensis</em> and <em>E. coli</em>. The diffused localization of CmWag31<sup>A102T</sup> can be restored by overexpression of CmPBPC in <em>C. michiganensis</em>, yet this restoration is not observed in <em>E. coli</em>. This result indicates that CmPBPC from <em>C. michiganensis</em> may not fully excute their function in <em>E. coli</em> due to species-specific differences.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100151"},"PeriodicalIF":6.2,"publicationDate":"2025-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144932135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-08-12DOI: 10.1016/j.tcsw.2025.100150
N.E. Mvubu
M. tuberculosis is a notorious global pathogen responsible for over a million fatalities annually. It has been estimated that one-third of the world's population is latently infected with M. tuberculosis; however, only ∼10 million individuals develop an active disease annually. The innate immune defence system is the first to encounter the bacilli and initiates a cascade of events to protect the host from developing tuberculosis. Innate immune cells such as pulmonary epithelial cells, alveolar macrophages, and dendritic cells express Toll-like Receptors (TLRs), C-type Lectin Receptors (CLRs), NOD-like Receptors (NLRs), Scavenger Receptors, Surfactant Proteins, RIG-I–like Receptors (RLRs), Complement Receptors, and Fc Receptors upon exposure to M. tuberculosis Pathogen-Associated Molecular Patterns (PAMPs). The interaction between host Pathogen Recognition Receptors (PRRs) and M. tuberculosis PAMPs results in the activation of several signalling pathways that initiate an inflammatory response through the production of cytokines and chemokines at the site of infection. This Surface Feature manuscript provides an up-to-date report on the expression of host PRRs in pulmonary epithelial cells, alveolar macrophages and dendritic cells and their interactions with M. tuberculosis PAMPs to initiate an inflammatory response at the site of infection. Furthermore, this manuscript sheds light on the role of this inflammatory response as a “double-edged sword” in the fight against M. tuberculosis infection. Understanding these interactions provides a directive for host-directed therapies to modulate the innate immune response.
{"title":"Innate immune recognition of Mycobacterium tuberculosis: receptor engagement and inflammatory outcomes at the site of infection","authors":"N.E. Mvubu","doi":"10.1016/j.tcsw.2025.100150","DOIUrl":"10.1016/j.tcsw.2025.100150","url":null,"abstract":"<div><div><em>M. tuberculosis</em> is a notorious global pathogen responsible for over a million fatalities annually. It has been estimated that one-third of the world's population is latently infected with <em>M. tuberculosis</em>; however, only ∼10 million individuals develop an active disease annually. The innate immune defence system is the first to encounter the bacilli and initiates a cascade of events to protect the host from developing tuberculosis. Innate immune cells such as pulmonary epithelial cells, alveolar macrophages, and dendritic cells express Toll-like Receptors (TLRs), C-type Lectin Receptors (CLRs), NOD-like Receptors (NLRs), Scavenger Receptors, Surfactant Proteins, RIG-I–like Receptors (RLRs), Complement Receptors, and Fc Receptors upon exposure to <em>M. tuberculosis</em> Pathogen-Associated Molecular Patterns (PAMPs). The interaction between host Pathogen Recognition Receptors (PRRs) and <em>M. tuberculosis</em> PAMPs results in the activation of several signalling pathways that initiate an inflammatory response through the production of cytokines and chemokines at the site of infection. This Surface Feature manuscript provides an up-to-date report on the expression of host PRRs in pulmonary epithelial cells, alveolar macrophages and dendritic cells and their interactions with <em>M. tuberculosis</em> PAMPs to initiate an inflammatory response at the site of infection. Furthermore, this manuscript sheds light on the role of this inflammatory response as a “double-edged sword” in the fight against <em>M. tuberculosis</em> infection. Understanding these interactions provides a directive for host-directed therapies to modulate the innate immune response.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100150"},"PeriodicalIF":6.2,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144878298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-07-03DOI: 10.1016/j.tcsw.2025.100149
Abayeneh Girma
A persistent increase in antimicrobial resistance presents a significant danger to global public health. The application of bactericidal phages that do not interfere with the body's natural flora becomes a promising approach to alternative treatments. This section offers an in-depth examination of the use of bacteriophage therapy in both laboratory and human trials for the treatment of specific bacterial infections. The benefits and hurdles of increasing the use of bacteriophages as a supplemental or alternative treatment for bacterial infections resistant to antibiotics are examined. The use of highly adaptable bacteriophage populations, combined with antibiotic chemical compounds, as molecular tools to combat rapidly evolving pathogenic bacteria in the host environment, presents significant virologic complexities. Pre-clinical studies, isolated clinical reports and a few randomized clinical trials have demonstrated that bacteriophages can be effective for treating bacterial infections that are resistant to multiple drugs. The capability of certain bacteriophages to reverse antibiotic resistance, as well as resistance to human complement and other bacteriophages seems to be a significant benefit of bacteriophage therapy, despite the predictable appearance of bacteriophage-resistant strains. Bacteriophages or specific products derived from them can improve antimicrobial effectiveness by decreasing bacteria's harmful properties through changes to fundamental bacterial structures, mainly their cell walls and membranes. Despite several ongoing issues regarding their practical use, it seems that bacteriophage-based treatments combined with antibiotics can serve as an effective solution to addressing the spread of antimicrobial resistance.
{"title":"Bacteriophages as an alternative strategy for the treatment of drug resistant bacterial infections: Current approaches and future perspectives","authors":"Abayeneh Girma","doi":"10.1016/j.tcsw.2025.100149","DOIUrl":"10.1016/j.tcsw.2025.100149","url":null,"abstract":"<div><div>A persistent increase in antimicrobial resistance presents a significant danger to global public health. The application of bactericidal phages that do not interfere with the body's natural flora becomes a promising approach to alternative treatments. This section offers an in-depth examination of the use of bacteriophage therapy in both laboratory and human trials for the treatment of specific bacterial infections. The benefits and hurdles of increasing the use of bacteriophages as a supplemental or alternative treatment for bacterial infections resistant to antibiotics are examined. The use of highly adaptable bacteriophage populations, combined with antibiotic chemical compounds, as molecular tools to combat rapidly evolving pathogenic bacteria in the host environment, presents significant virologic complexities. Pre-clinical studies, isolated clinical reports and a few randomized clinical trials have demonstrated that bacteriophages can be effective for treating bacterial infections that are resistant to multiple drugs. The capability of certain bacteriophages to reverse antibiotic resistance, as well as resistance to human complement and other bacteriophages seems to be a significant benefit of bacteriophage therapy, despite the predictable appearance of bacteriophage-resistant strains. Bacteriophages or specific products derived from them can improve antimicrobial effectiveness by decreasing bacteria's harmful properties through changes to fundamental bacterial structures, mainly their cell walls and membranes. Despite several ongoing issues regarding their practical use, it seems that bacteriophage-based treatments combined with antibiotics can serve as an effective solution to addressing the spread of antimicrobial resistance.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"14 ","pages":"Article 100149"},"PeriodicalIF":0.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144570124","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-06-01DOI: 10.1016/j.tcsw.2025.100147
Paul Vogel , Staffan Persson , Guillermo Moreno-Pescador , Lise C. Noack
Plants sense their environment at the cell surface, i.e. the plasma membrane, where extracellular signals are perceived and transduced. Together with the cortical cytoskeleton and the cell wall, membrane lipids can influence these processes by acting on protein dynamics at the plasma membrane. Among these lipids, sterols regulate membrane fluidity and thus, protein functions. However, plant sterols are diverse in structure and particularly difficult to study due to technical limitations. Nevertheless, advances in sterol imaging, sterol-protein interaction studies, and sterol perturbation methods have resulted in a better understanding of their functions in plant development and physiology. Here we summarize the current knowledge and the latest breakthroughs, and discuss future challenges, in the field of plant sterol biology and cell surface organization.
{"title":"Sterols in plant biology – Advances in studying membrane dynamics","authors":"Paul Vogel , Staffan Persson , Guillermo Moreno-Pescador , Lise C. Noack","doi":"10.1016/j.tcsw.2025.100147","DOIUrl":"10.1016/j.tcsw.2025.100147","url":null,"abstract":"<div><div>Plants sense their environment at the cell surface, i.e. the plasma membrane, where extracellular signals are perceived and transduced. Together with the cortical cytoskeleton and the cell wall, membrane lipids can influence these processes by acting on protein dynamics at the plasma membrane. Among these lipids, sterols regulate membrane fluidity and thus, protein functions. However, plant sterols are diverse in structure and particularly difficult to study due to technical limitations. Nevertheless, advances in sterol imaging, sterol-protein interaction studies, and sterol perturbation methods have resulted in a better understanding of their functions in plant development and physiology. Here we summarize the current knowledge and the latest breakthroughs, and discuss future challenges, in the field of plant sterol biology and cell surface organization.</div></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"13 ","pages":"Article 100147"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144189297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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