Pub Date : 2024-06-01DOI: 10.1016/j.tcsw.2024.100128
Qinxi Ma , Arnab Pradhan , Ian Leaves , Emer Hickey , Elena Roselletti , Ivy Dambuza , Daniel E. Larcombe , Leandro Jose de Assis , Duncan Wilson , Lars P. Erwig , Mihai G. Netea , Delma S. Childers , Gordon D. Brown , Neil A.R. Gow , Alistair J.P. Brown
Host recognition of the pathogen-associated molecular pattern (PAMP), β-1,3-glucan, plays a major role in antifungal immunity. β-1,3-glucan is an essential component of the inner cell wall of the opportunistic pathogen Candida albicans. Most β-1,3-glucan is shielded by the outer cell wall layer of mannan fibrils, but some can become exposed at the cell surface. In response to host signals such as lactate, C. albicans shaves the exposed β-1,3-glucan from its cell surface, thereby reducing the ability of innate immune cells to recognise and kill the fungus. We have used sets of barcoded xog1 and eng1 mutants to compare the impacts of the secreted β-glucanases Xog1 and Eng1 upon C. albicans in vitro and in vivo. Flow cytometry of Fc-dectin-1-stained strains revealed that Eng1 plays the greater role in lactate-induced β-1,3-glucan masking. Transmission electron microscopy and stress assays showed that neither Eng1 nor Xog1 are essential for cell wall maintenance, but the inactivation of either enzyme compromised fungal adhesion to gut and vaginal epithelial cells. Competitive barcode sequencing suggested that neither Eng1 nor Xog1 strongly influence C. albicans fitness during systemic infection or vaginal colonisation in mice. However, the deletion of XOG1 enhanced C. albicans fitness during gut colonisation. We conclude that both Eng1 and Xog1 exert subtle effects on the C. albicans cell surface that influence fungal adhesion to host cells and that affect fungal colonisation in certain host niches.
{"title":"Impact of secreted glucanases upon the cell surface and fitness of Candida albicans during colonisation and infection","authors":"Qinxi Ma , Arnab Pradhan , Ian Leaves , Emer Hickey , Elena Roselletti , Ivy Dambuza , Daniel E. Larcombe , Leandro Jose de Assis , Duncan Wilson , Lars P. Erwig , Mihai G. Netea , Delma S. Childers , Gordon D. Brown , Neil A.R. Gow , Alistair J.P. Brown","doi":"10.1016/j.tcsw.2024.100128","DOIUrl":"10.1016/j.tcsw.2024.100128","url":null,"abstract":"<div><p>Host recognition of the pathogen-associated molecular pattern (PAMP), β-1,3-glucan, plays a major role in antifungal immunity. β-1,3-glucan is an essential component of the inner cell wall of the opportunistic pathogen <em>Candida albicans</em>. Most β-1,3-glucan is shielded by the outer cell wall layer of mannan fibrils, but some can become exposed at the cell surface. In response to host signals such as lactate, <em>C. albicans</em> shaves the exposed β-1,3-glucan from its cell surface, thereby reducing the ability of innate immune cells to recognise and kill the fungus. We have used sets of barcoded <em>xog1</em> and <em>eng1</em> mutants to compare the impacts of the secreted β-glucanases Xog1 and Eng1 upon <em>C. albicans in vitro</em> and <em>in vivo</em>. Flow cytometry of Fc-dectin-1-stained strains revealed that Eng1 plays the greater role in lactate-induced β-1,3-glucan masking. Transmission electron microscopy and stress assays showed that neither Eng1 nor Xog1 are essential for cell wall maintenance, but the inactivation of either enzyme compromised fungal adhesion to gut and vaginal epithelial cells. Competitive barcode sequencing suggested that neither Eng1 nor Xog1 strongly influence <em>C. albicans</em> fitness during systemic infection or vaginal colonisation in mice. However, the deletion of <em>XOG1</em> enhanced <em>C. albicans</em> fitness during gut colonisation. We conclude that both Eng1 and Xog1 exert subtle effects on the <em>C. albicans</em> cell surface that influence fungal adhesion to host cells and that affect fungal colonisation in certain host niches.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100128"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000100/pdfft?md5=65705da5b1785db1447a44b255bd78e8&pid=1-s2.0-S2468233024000100-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141275629","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-05-21DOI: 10.1016/j.tcsw.2024.100126
Lige Tong , Yunaying Li , Xinke Lou , Bin Wang , Cheng Jin , Wenxia Fang
Cell wall biomass, Earth’s most abundant natural resource, holds significant potential for sustainable biofuel production. Composed of cellulose, hemicellulose, lignin, pectin, and other polymers, the plant cell wall provides essential structural support to diverse organisms in nature. In contrast, non-plant species like insects, crustaceans, and fungi rely on chitin as their primary structural polysaccharide. The saprophytic fungus Aspergillus fumigatus has been widely recognized for its adaptability to various environmental conditions. It achieves this by secreting different cell wall biomass degradation enzymes to obtain essential nutrients. This review compiles a comprehensive collection of cell wall degradation enzymes derived from A. fumigatus, including cellulases, hemicellulases, various chitin degradation enzymes, and other polymer degradation enzymes. Notably, these enzymes exhibit biochemical characteristics such as temperature tolerance or acid adaptability, indicating their potential applications across a spectrum of industries.
{"title":"Powerful cell wall biomass degradation enzymatic system from saprotrophic Aspergillus fumigatus","authors":"Lige Tong , Yunaying Li , Xinke Lou , Bin Wang , Cheng Jin , Wenxia Fang","doi":"10.1016/j.tcsw.2024.100126","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100126","url":null,"abstract":"<div><p>Cell wall biomass, Earth’s most abundant natural resource, holds significant potential for sustainable biofuel production. Composed of cellulose, hemicellulose, lignin, pectin, and other polymers, the plant cell wall provides essential structural support to diverse organisms in nature. In contrast, non-plant species like insects, crustaceans, and fungi rely on chitin as their primary structural polysaccharide. The saprophytic fungus <em>Aspergillus fumigatus</em> has been widely recognized for its adaptability to various environmental conditions. It achieves this by secreting different cell wall biomass degradation enzymes to obtain essential nutrients. This review compiles a comprehensive collection of cell wall degradation enzymes derived from <em>A. fumigatus</em>, including cellulases, hemicellulases, various chitin degradation enzymes, and other polymer degradation enzymes. Notably, these enzymes exhibit biochemical characteristics such as temperature tolerance or acid adaptability, indicating their potential applications across a spectrum of industries.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100126"},"PeriodicalIF":0.0,"publicationDate":"2024-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000082/pdfft?md5=4b3a2fb15bf2f3b050c9a7cf76d15337&pid=1-s2.0-S2468233024000082-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141089975","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Non-tuberculosis mycobacteria (NTM) can form biofilms on diverse artificial surfaces. In the present study, we induced NTM biofilm formation on materials used in various medical devices, evaluated the total amount of biofilm, and observed the ultrastructure by scanning electron microscopy.
{"title":"Formative evaluation and structural analysis of non-tuberculosis mycobacterial biofilm using material pieces","authors":"Kentaro Yamamoto , Shota Torigoe , Hirotaka Kobayashi","doi":"10.1016/j.tcsw.2024.100125","DOIUrl":"10.1016/j.tcsw.2024.100125","url":null,"abstract":"<div><p>Non-tuberculosis mycobacteria (NTM) can form biofilms on diverse artificial surfaces. In the present study, we induced NTM biofilm formation on materials used in various medical devices, evaluated the total amount of biofilm, and observed the ultrastructure by scanning electron microscopy.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100125"},"PeriodicalIF":0.0,"publicationDate":"2024-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000070/pdfft?md5=ee4bdff164161364e8855ce5b11df75e&pid=1-s2.0-S2468233024000070-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141034326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-04-04DOI: 10.1016/j.tcsw.2024.100124
Patricia Fernández-Calvo , Gemma López , Marina Martín-Dacal , Meriem Aitouguinane , Cristian Carrasco-López , Sara González-Bodí , Laura Bacete , Hugo Mélida , Andrea Sánchez-Vallet , Antonio Molina
Pattern-Triggered Immunity (PTI) in plants is activated upon recognition by Pattern Recognition Receptors (PRRs) of Damage- and Microbe-Associated Molecular Patterns (DAMPs and MAMPs) from plants or microorganisms, respectively. An increasing number of identified DAMPs/MAMPs are carbohydrates from plant cell walls and microbial extracellular layers, which are perceived by plant PRRs, such as LysM and Leucine Rich Repeat-Malectin (LRR-MAL) receptor kinases (RKs). LysM-RKs (e.g. CERK1, LYK4 and LYK5) are needed for recognition of fungal MAMP chitohexaose (β-1,4-D-(GlcNAc)6, CHI6), whereas IGP1/CORK1, IGP3 and IGP4 LRR-MAL RKs are required for perception of β-glucans, like cellotriose (β-1,4-D-(Glc)3, CEL3) and mixed-linked glucans. We have explored the diversity of carbohydrates perceived by Arabidopsis thaliana seedlings by determining PTI responses upon treatment with different oligosaccharides and polysaccharides. These analyses revealed that plant oligosaccharides from xylans [β-1,4-D-(xylose)4 (XYL4)], glucuronoxylans and α-1,4-glucans, and polysaccharides from plants and seaweeds activate PTI. Cross-elicitation experiments of XYL4 with other glycans showed that the mechanism of recognition of XYL4 and the DAMP 33-α-L-arabinofuranosyl-xylotetraose (XA3XX) shares some features with that of CEL3 but differs from that of CHI6. Notably, XYL4 and XA3XX perception is impaired in igp1/cork1, igp3 and igp4 mutants, and almost not affected in cerk1 lyk4 lyk5 triple mutant. XYL4 perception is conserved in different plant species since XYL4 pre-treatment triggers enhanced disease resistance in tomato to Pseudomonas syringae pv tomato DC3000 and PTI responses in wheat. These results expand the number of glycans triggering plant immunity and support IGP1/CORK1, IGP3 and IGP4 relevance in Arabidopsis thaliana glycans perception and PTI activation.
Significance Statement
The characterization of plant immune mechanisms involved in the perception of carbohydrate-based structures recognized as DAMPs/MAMPs is needed to further understand plant disease resistance modulation. We show here that IGP1/CORK1, IGP3 and IGP4 LRR-MAL RKs are required for the perception of carbohydrate-based DAMPs β-1,4-D-(xylose)4 (XYL4) and 33-α-L-arabinofuranosyl-xylotetraose (XA3XX), further expanding the function of these LRR-MAL RKs in plant glycan perception and immune activation.
{"title":"Leucine rich repeat-malectin receptor kinases IGP1/CORK1, IGP3 and IGP4 are required for arabidopsis immune responses triggered by β-1,4-D-Xylo-oligosaccharides from plant cell walls","authors":"Patricia Fernández-Calvo , Gemma López , Marina Martín-Dacal , Meriem Aitouguinane , Cristian Carrasco-López , Sara González-Bodí , Laura Bacete , Hugo Mélida , Andrea Sánchez-Vallet , Antonio Molina","doi":"10.1016/j.tcsw.2024.100124","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100124","url":null,"abstract":"<div><p>Pattern-Triggered Immunity (PTI) in plants is activated upon recognition by Pattern Recognition Receptors (PRRs) of Damage- and Microbe-Associated Molecular Patterns (DAMPs and MAMPs) from plants or microorganisms, respectively. An increasing number of identified DAMPs/MAMPs are carbohydrates from plant cell walls and microbial extracellular layers, which are perceived by plant PRRs, such as LysM and Leucine Rich Repeat-Malectin (LRR-MAL) receptor kinases (RKs). LysM-RKs (e.g. CERK1, LYK4 and LYK5) are needed for recognition of fungal MAMP chitohexaose (β-1,4-D-(GlcNAc)<sub>6</sub>, CHI6), whereas IGP1/CORK1, IGP3 and IGP4 LRR-MAL RKs are required for perception of β-glucans, like cellotriose (β-1,4-D-(Glc)<sub>3</sub>, CEL3) and mixed-linked glucans. We have explored the diversity of carbohydrates perceived by <em>Arabidopsis thaliana</em> seedlings by determining PTI responses upon treatment with different oligosaccharides and polysaccharides. These analyses revealed that plant oligosaccharides from xylans [β-1,4-D-(xylose)<sub>4</sub> (XYL4)], glucuronoxylans and α-1,4-glucans, and polysaccharides from plants and seaweeds activate PTI. Cross-elicitation experiments of XYL4 with other glycans showed that the mechanism of recognition of XYL4 and the DAMP 3<sup>3</sup>-α-L-arabinofuranosyl-xylotetraose (XA<sub>3</sub>XX) shares some features with that of CEL3 but differs from that of CHI6. Notably, XYL4 and XA<sub>3</sub>XX perception is impaired in <em>igp1/cork1, igp3</em> and <em>igp4</em> mutants, and almost not affected in <em>cerk1 lyk4 lyk5</em> triple mutant. XYL4 perception is conserved in different plant species since XYL4 pre-treatment triggers enhanced disease resistance in tomato to <em>Pseudomonas syringae</em> pv <em>tomato</em> DC3000 and PTI responses in wheat. These results expand the number of glycans triggering plant immunity and support IGP1/CORK1, IGP3 and IGP4 relevance in <em>Arabidopsis thaliana</em> glycans perception and PTI activation.</p></div><div><h3>Significance Statement</h3><p>The characterization of plant immune mechanisms involved in the perception of carbohydrate-based structures recognized as DAMPs/MAMPs is needed to further understand plant disease resistance modulation. We show here that IGP1/CORK1, IGP3 and IGP4 LRR-MAL RKs are required for the perception of carbohydrate-based DAMPs β-1,4-D-(xylose)<sub>4</sub> (XYL4) and 3<sup>3</sup>-α-L-arabinofuranosyl-xylotetraose (XA<sub>3</sub>XX), further expanding the function of these LRR-MAL RKs in plant glycan perception and immune activation.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100124"},"PeriodicalIF":0.0,"publicationDate":"2024-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000069/pdfft?md5=b4df742d1e119c978479e3078e773fde&pid=1-s2.0-S2468233024000069-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140533453","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-03-25DOI: 10.1016/j.tcsw.2024.100123
Theodore J. Kottom , Eva M. Carmona , Bernd Lepenies , Andrew H. Limper
Herein, this manuscript explores the significance of the phosphoglucomutase (PGM) enzyme in Pneumocystis spp., focusing on its role in fungal surface mannoprotein formation. Through expression of the Pneumocystis murina Pmpgm2 in a Saccharomyces cerevisiae pgm2Δ strain, we demonstrate restoration of binding to the mannose receptor (MR) and macrophages to wildtype yeast levels in this complemented strain. Gas Chromatography-Mass Spectroscopy (GC-MS) confirmed reduced mannose content in the pgm2Δ yeast strain compared to the wild-type and complemented Pmpgm2 cDNA-expressing strains. This study underscores fungal PGM function in dolichol glucosyl phosphate biosynthesis, crucial for proper cell wall mannoprotein formation. Furthermore, highlighting the conservation of targetable cysteine residues across fungal pathogens, PGM inhibition maybe a potential therapeutic strategy against a broad spectrum of fungal infections.
{"title":"Metabolic modulation: Pneumocystis phosphoglucomutase is a target influencing host recognition","authors":"Theodore J. Kottom , Eva M. Carmona , Bernd Lepenies , Andrew H. Limper","doi":"10.1016/j.tcsw.2024.100123","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100123","url":null,"abstract":"<div><p>Herein, this manuscript explores the significance of the phosphoglucomutase (PGM) enzyme in <em>Pneumocystis</em> spp., focusing on its role in fungal surface mannoprotein formation. Through expression of the <em>Pneumocystis murina Pmpgm2</em> in a <em>Saccharomyces cerevisiae pgm2Δ</em> strain, we demonstrate restoration of binding to the mannose receptor (MR) and macrophages to wildtype yeast levels in this complemented strain. Gas Chromatography-Mass Spectroscopy (GC-MS) confirmed reduced mannose content in the <em>pgm2Δ</em> yeast strain compared to the wild-type and complemented <em>Pmpgm2</em> cDNA-expressing strains. This study underscores fungal PGM function in dolichol glucosyl phosphate biosynthesis, crucial for proper cell wall mannoprotein formation. Furthermore, highlighting the conservation of targetable cysteine residues across fungal pathogens, PGM inhibition maybe a potential therapeutic strategy against a broad spectrum of fungal infections.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100123"},"PeriodicalIF":0.0,"publicationDate":"2024-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000057/pdfft?md5=cd9f34cba7959a467ab1e8b22534c651&pid=1-s2.0-S2468233024000057-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140296340","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-02-21DOI: 10.1016/j.tcsw.2024.100122
Sarah M. Batt , Katherine A. Abrahams , Gurdyal S. Besra
{"title":"Top five unanswered questions in bacterial cell wall research","authors":"Sarah M. Batt , Katherine A. Abrahams , Gurdyal S. Besra","doi":"10.1016/j.tcsw.2024.100122","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100122","url":null,"abstract":"","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100122"},"PeriodicalIF":0.0,"publicationDate":"2024-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000045/pdfft?md5=2eeff22755cc33280315a7452506081f&pid=1-s2.0-S2468233024000045-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139936454","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-02-13DOI: 10.1016/j.tcsw.2024.100121
Wout Boerjan , Vincent Burlat , Daniel J. Cosgrove , Christophe Dunand , Paul Dupree , Kalina T. Haas , Gwyneth Ingram , Elisabeth Jamet , Debra Mohnen , Steven Moussu , Alexis Peaucelle , Staffan Persson , Cătălin Voiniciuc , Herman Höfte
Plant cell wall researchers were asked their view on what the major unanswered questions are in their field. This article summarises the feedback that was received from them in five questions. In this issue you can find equivalent syntheses for researchers working on bacterial, unicellular parasite and fungal systems.
{"title":"Top five unanswered questions in plant cell surface research","authors":"Wout Boerjan , Vincent Burlat , Daniel J. Cosgrove , Christophe Dunand , Paul Dupree , Kalina T. Haas , Gwyneth Ingram , Elisabeth Jamet , Debra Mohnen , Steven Moussu , Alexis Peaucelle , Staffan Persson , Cătălin Voiniciuc , Herman Höfte","doi":"10.1016/j.tcsw.2024.100121","DOIUrl":"10.1016/j.tcsw.2024.100121","url":null,"abstract":"<div><p>Plant cell wall researchers were asked their view on what the major unanswered questions are in their field. This article summarises the feedback that was received from them in five questions. In this issue you can find equivalent syntheses for researchers working on bacterial, unicellular parasite and fungal systems.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100121"},"PeriodicalIF":0.0,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000033/pdfft?md5=e30e865172f8a5fc982da0e4fca9f0eb&pid=1-s2.0-S2468233024000033-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139871611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-01-14DOI: 10.1016/j.tcsw.2024.100120
Nur Afrina Muhamad Hendri , Nur Asyura Nor Amdan , Shelly Olevia Dounis , Norzarila Sulaiman Najib , Santhana Raj Louis
Background
Many studies reported the effects of antibiotic exposure on E. coli bacterial growth and cell modification. However, scarce descriptive information on ultrastructural effects upon exposure of commercial antibiotics.
Methods
This study described the morphological and ultrastructural alterations caused by selected antibiotics (amoxicillin-clavulanate, ceftriaxone, polymyxin B, colistin, gentamicin, and amikacin) that targeted cell wall, plasma membrane, and cytoplasmic density, and also proteins synthesis. We determined extracellular morphological changes of exposure through scanning electron microscopy (FESEM) and intracellular activities through transmission electron microscopy (TEM) investigation.
Results
FESEM and TEM micrograph of E. coli exposed with selected antibiotics shows ultrastructural changes in beta-lactam class (amoxicillin-clavulanate, ceftriaxone) elongated the cells as the cell wall was altered as it inhibits bacterial cell wall synthesis, polymyxin class (polymyxin B, colistin) had plasmid and curli-fimbriae as it breaking down the plasma/cytoplasmic membrane, and aminoglycoside class (gentamicin, and amikacin) reduced ribosome concentration as it inhibits bacterial protein synthesis by binding to 30 s ribosomes.
Conclusion
Morphological and ultrastructural alterations of E. coli’s mechanism of actions were translated and depicted. This study could be reference for characterization studies for morphological and ultrastructural of E. coli upon exposure to antimicrobial agents.
背景许多研究都报道了抗生素暴露对大肠杆菌生长和细胞改造的影响。本研究描述了某些抗生素(阿莫西林-克拉维酸、头孢曲松、多粘菌素 B、大肠杆菌素、庆大霉素和阿米卡星)针对细胞壁、质膜和细胞质密度以及蛋白质合成所引起的形态学和超微结构改变。我们通过扫描电子显微镜(FESEM)和透射电子显微镜(TEM)研究确定了暴露后的细胞外形态变化和细胞内活性。大肠杆菌暴露于某些抗生素后,其超微结构发生了变化:β-内酰胺类(阿莫西林-克拉维酸、头孢曲松)由于抑制了细菌细胞壁的合成而改变了细胞壁,使细胞变长;多粘菌素类(多粘菌素 B、大肠菌素)由于抑制了细菌细胞壁的合成而改变了细胞壁,使细胞变长;多粘菌素类(多粘菌素 B、大肠菌素)由于抑制了细菌细胞壁的合成而改变了细胞壁,使细胞变长、氨基糖苷类(庆大霉素和阿米卡星)通过与 30 s 核糖体结合抑制细菌蛋白质合成,从而降低核糖体浓度。结论 对大肠杆菌作用机制的形态学和超微结构改变进行了翻译和描述。这项研究可作为大肠杆菌接触抗菌剂后形态学和超微结构特征研究的参考。
{"title":"Ultrastructural and morphological studies on variables affecting Escherichia coli with selected commercial antibiotics","authors":"Nur Afrina Muhamad Hendri , Nur Asyura Nor Amdan , Shelly Olevia Dounis , Norzarila Sulaiman Najib , Santhana Raj Louis","doi":"10.1016/j.tcsw.2024.100120","DOIUrl":"https://doi.org/10.1016/j.tcsw.2024.100120","url":null,"abstract":"<div><h3>Background</h3><p>Many studies reported the effects of antibiotic exposure on <em>E. coli</em> bacterial growth and cell modification. However, scarce descriptive information on ultrastructural effects upon exposure of commercial antibiotics.</p></div><div><h3>Methods</h3><p>This study described the morphological and ultrastructural alterations caused by selected antibiotics (amoxicillin-clavulanate, ceftriaxone, polymyxin B, colistin, gentamicin, and amikacin) that targeted cell wall, plasma membrane, and cytoplasmic density, and also proteins synthesis. We determined extracellular morphological changes of exposure through scanning electron microscopy (FESEM) and intracellular activities through transmission electron microscopy (TEM) investigation.</p></div><div><h3>Results</h3><p>FESEM and TEM micrograph of <em>E. coli</em> exposed with selected antibiotics shows ultrastructural changes in beta-lactam class (amoxicillin-clavulanate, ceftriaxone) elongated the cells as the cell wall was altered as it inhibits bacterial cell wall synthesis, polymyxin class (polymyxin B, colistin) had plasmid and curli-fimbriae as it breaking down the plasma/cytoplasmic membrane, and aminoglycoside class (gentamicin, and amikacin) reduced ribosome concentration as it inhibits bacterial protein synthesis by binding to 30 s ribosomes.</p></div><div><h3>Conclusion</h3><p>Morphological and ultrastructural alterations of <em>E. coli</em>’s mechanism of actions were translated and depicted. This study could be reference for characterization studies for morphological and ultrastructural of <em>E. coli</em> upon exposure to antimicrobial agents.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"11 ","pages":"Article 100120"},"PeriodicalIF":0.0,"publicationDate":"2024-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233024000021/pdfft?md5=e47390b00c583a3b62ca71468a7a1a5f&pid=1-s2.0-S2468233024000021-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139503891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-11-25DOI: 10.1016/j.tcsw.2023.100117
Dasmeet Kaur , Michael A. Held , Yuan Zhang , Diana Moreira , Silvia Coimbra , Allan M. Showalter
Arabinogalactan-proteins (AGPs) are a family of hyperglycosylated hydroxyproline-rich cell wall proteins found throughout the plant kingdom. To date, eight Hydroxyproline-galactosyltransferases (Hyp-GALTs), named GALT2-GALT9, are known to catalyze the addition of the first galactose sugar to Hyp residues in AGP protein cores. The generation and characterization of galt23456789 octuple mutants using CRISPR-Cas9 gene editing technology, provided strong reverse genetic evidence that AG glycans are essential for normal vegetative and reproductive growth, as these mutants demonstrated stunted growth, greatly delayed flowering and significant defects in floral organ development and morphogenesis. Compared to the lower seed set of galt25789 quintuple mutants being more so contributed by female gametophytic defects, dramatically low seed-set of octuple mutants was largely due to impaired male reproductive function, specifically due to shorter filaments, delayed anther dehiscence, and large decreases in pollen quantity and viability. Octuple mutant pollen had severely distorted reticulate exine, tectum patterning and intine thickness. Reduced amounts of galactose and arabinose in overall lower amounts of β-Yariv precipitated AGPs illustrated how biological functions of AGPs are affected by abnormal glycosylation.
{"title":"Knockout of eight hydroxyproline-O-galactosyltransferases cause multiple vegetative and reproductive growth defects","authors":"Dasmeet Kaur , Michael A. Held , Yuan Zhang , Diana Moreira , Silvia Coimbra , Allan M. Showalter","doi":"10.1016/j.tcsw.2023.100117","DOIUrl":"https://doi.org/10.1016/j.tcsw.2023.100117","url":null,"abstract":"<div><p>Arabinogalactan-proteins (AGPs) are a family of hyperglycosylated hydroxyproline-rich cell wall proteins found throughout the plant kingdom. To date, eight Hydroxyproline-galactosyltransferases (Hyp-GALTs), named GALT2-GALT9, are known to catalyze the addition of the first galactose sugar to Hyp residues in AGP protein cores. The generation and characterization of <em>galt23456789</em> octuple mutants using CRISPR-Cas9 gene editing technology, provided strong reverse genetic evidence that AG glycans are essential for normal vegetative and reproductive growth, as these mutants demonstrated stunted growth, greatly delayed flowering and significant defects in floral organ development and morphogenesis. Compared to the lower seed set of <em>galt25789</em> quintuple mutants being more so contributed by female gametophytic defects, dramatically low seed-set of octuple mutants was largely due to impaired male reproductive function, specifically due to shorter filaments, delayed anther dehiscence, and large decreases in pollen quantity and viability. Octuple mutant pollen had severely distorted reticulate exine, tectum patterning and intine thickness. Reduced amounts of galactose and arabinose in overall lower amounts of β-Yariv precipitated AGPs illustrated how biological functions of AGPs are affected by abnormal glycosylation.</p></div>","PeriodicalId":36539,"journal":{"name":"Cell Surface","volume":"10 ","pages":"Article 100117"},"PeriodicalIF":0.0,"publicationDate":"2023-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2468233023000245/pdfft?md5=97a2b425d59c79579fff34e40dcd748e&pid=1-s2.0-S2468233023000245-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138454011","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}