php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php). Technology advancements in antibody purification
{"title":"Technology advancements in antibody purification","authors":"C. Murphy, T. Devine, R. O’Kennedy","doi":"10.2147/ANTI.S64762","DOIUrl":"https://doi.org/10.2147/ANTI.S64762","url":null,"abstract":"php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php). Technology advancements in antibody purification","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"6 1","pages":"17-32"},"PeriodicalIF":0.0,"publicationDate":"2016-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S64762","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302973","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}
Neutralizing antibodies (NAbs) are an essential part of the human immune response that involves an intricate relationship between the innate and adaptive immune system to pre- vent infection. The appearance of NAbs is a hallmark of viral infection in patients with HIV, dengue, hepatitis C virus, Ebola, and influenza. These viruses are characterized by high genetic diversity of viral epitopes arising due to a high replication rate and an error-prone replication machinery. In general, almost all infected individuals develop strain-specific NAbs in a fairly short period of time. In contrast, broadly neutralizing antibodies (bNAbs) show subdominant responses and are found only in a subset of patients, typically after a lengthy period of infection. Epitopes targeted by specific NAbs and bNAbs evolved thereafter provide useful information for vaccine design. In this review, we discuss the isolation and utility of bNAbs against HIV-1, dengue, hepatitis C virus, influenza, and Ebola. Passive antibody therapy and the economics of NAb therapy are also discussed.
{"title":"Broadly neutralizing antibodies for therapy of viral infections","authors":"Sankaranarayanan Srinivasan, Maloy Ghosh, Sunit Maity, Raghavan Varadarajan","doi":"10.2147/ANTI.S92190","DOIUrl":"https://doi.org/10.2147/ANTI.S92190","url":null,"abstract":"Neutralizing antibodies (NAbs) are an essential part of the human immune response that involves an intricate relationship between the innate and adaptive immune system to pre- vent infection. The appearance of NAbs is a hallmark of viral infection in patients with HIV, dengue, hepatitis C virus, Ebola, and influenza. These viruses are characterized by high genetic diversity of viral epitopes arising due to a high replication rate and an error-prone replication machinery. In general, almost all infected individuals develop strain-specific NAbs in a fairly short period of time. In contrast, broadly neutralizing antibodies (bNAbs) show subdominant responses and are found only in a subset of patients, typically after a lengthy period of infection. Epitopes targeted by specific NAbs and bNAbs evolved thereafter provide useful information for vaccine design. In this review, we discuss the isolation and utility of bNAbs against HIV-1, dengue, hepatitis C virus, influenza, and Ebola. Passive antibody therapy and the economics of NAb therapy are also discussed.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"6 1","pages":"1-15"},"PeriodicalIF":0.0,"publicationDate":"2016-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S92190","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68303094","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}
{"title":"Antibody-based arrays in disease proteomics","authors":"Daniel A Guthy, Hans Voshol","doi":"10.2147/ANTI.S53335","DOIUrl":"https://doi.org/10.2147/ANTI.S53335","url":null,"abstract":"","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"5 1","pages":"15-25"},"PeriodicalIF":0.0,"publicationDate":"2015-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S53335","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302561","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}
Les integrons sont des structures genetiques lineaires d'ADN qui servent a la capture de genes et de vecteurs d'expression. La structure basique d'un integron inclut : une enzyme integrase appartenant a la famille des recombinases specifiques de type, un promoteur, et un site d'insertion attI, auquel de l'ADN additionnel sous forme de cassettes de genes est insere par l'action de l'integrase. Les integrons de Classe I sont les plus communs et consistent normalement en 2 segments conserves d'ADN localise de chaque cote des cassettes de genes, la plupart correspondant a des genes de resistance aux antibiotiques. Ces cassettes de genes sont capables d'insertion a mediation integrase ou de deletion entre les segments conserves dans differents ordres et combinaisons. Les integrons agissent comme vecteurs en apportant un promoteur pour la transcription (expression) des cassettes de genes integres. Plus de 60 differentes cassettes de genes ont ete decrites, conferant la resistance vis-a-vis de nombreuses familles d'antibiotiques utilises contre les bacteries a Gram negatif, ces integrons etant trouves chez les souches cliniques de Gram negatifs dans le monde entier. Ils sont associes plus particulierement a la resistance aux aminoglycosides des souches d'origine clinique. L'emergence recente d'integrons hebergeant la resistance aux carbapenemes constitue un developpement reellement menacant. Il apparait clairement que les integrons permettent aux bacteries une adaptation continue et rapide a l'emploi en clinique de nouveaux antibiotiques, par l'acquisition de nouvelles cassettes de genes de resistance. En plus de leur role dans la dissemination de resistance aux antibiotiques, la mise en evidence de structures dites « super-integron » suggere que les integrons fonctionnent en tant que systemes de « gene-capture » plus generaux pour l'adaptation et l'evolution des bacteries.
{"title":"Advances in the development of antibody-based immunotherapy against prion disease","authors":"Huiying Gu, R. Dodel, M. Farlow, Yansheng Du","doi":"10.2147/ANTI.S53336","DOIUrl":"https://doi.org/10.2147/ANTI.S53336","url":null,"abstract":"Les integrons sont des structures genetiques lineaires d'ADN qui servent a la capture de genes et de vecteurs d'expression. La structure basique d'un integron inclut : une enzyme integrase appartenant a la famille des recombinases specifiques de type, un promoteur, et un site d'insertion attI, auquel de l'ADN additionnel sous forme de cassettes de genes est insere par l'action de l'integrase. Les integrons de Classe I sont les plus communs et consistent normalement en 2 segments conserves d'ADN localise de chaque cote des cassettes de genes, la plupart correspondant a des genes de resistance aux antibiotiques. Ces cassettes de genes sont capables d'insertion a mediation integrase ou de deletion entre les segments conserves dans differents ordres et combinaisons. Les integrons agissent comme vecteurs en apportant un promoteur pour la transcription (expression) des cassettes de genes integres. Plus de 60 differentes cassettes de genes ont ete decrites, conferant la resistance vis-a-vis de nombreuses familles d'antibiotiques utilises contre les bacteries a Gram negatif, ces integrons etant trouves chez les souches cliniques de Gram negatifs dans le monde entier. Ils sont associes plus particulierement a la resistance aux aminoglycosides des souches d'origine clinique. L'emergence recente d'integrons hebergeant la resistance aux carbapenemes constitue un developpement reellement menacant. Il apparait clairement que les integrons permettent aux bacteries une adaptation continue et rapide a l'emploi en clinique de nouveaux antibiotiques, par l'acquisition de nouvelles cassettes de genes de resistance. En plus de leur role dans la dissemination de resistance aux antibiotiques, la mise en evidence de structures dites « super-integron » suggere que les integrons fonctionnent en tant que systemes de « gene-capture » plus generaux pour l'adaptation et l'evolution des bacteries.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"4 1","pages":"45-55"},"PeriodicalIF":0.0,"publicationDate":"2014-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S53336","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302220","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}
Serologic assays detecting antibodies to Borrelia burgdorferi are useful in the routine diagnosis of Lyme disease. Despite the presence of new and improved assays, current laboratory diagnosis still requires optimization. The variety of genospecies and their different geographic distributions are the reasons why standards and recommendations are not the same for all of the main geographic regions, ie, USA, Asia, and Europe. Moreover, the variety and variability of antigens represents a significant challenge in assay design. This is due to the various antigens among the genospecies responsible for Lyme borreliosis; the changing antigens presented during infection; and the variability of single antigens. This review article discusses the immunologic response in Lyme disease over time, and the advantages and disadvantages of existing serological tests. Two tier testing is also introduced. Antigens useful for diagnosis, the properties of individual antigens and their appearance in infection especially the antigens appearing during mammalian infection, so-called “in vivo” antigens are introduced. To determine antibodies confirming infection in the nervous system, the same restrictions with regard to interpretation of enzyme-linked immunosorbent assay results in serum apply to cerebrospinal fluid. Furthermore, concentrations of antibodies in the two compartments, ie, blood and cerebrospinal fluid, are variable depending on compartmentalization (anatomic sequestration) and immunologic phenomena at immunologically privileged sites, such as the intrathecal space. To confirm neuroborreliosis, synthesis of antibodies in cerebrospinal fluid, should be measured in the form of a so-called antibody index. Further studies should focus on detecting the lowest concentration of antibodies and looking for useful new antigens, and the relationship between composition of such antigens and the patient’s clinical status.
{"title":"Antibody-based techniques for detection of Lyme disease: a challenging issue","authors":"J. Zajkowska","doi":"10.2147/ANTI.S39718","DOIUrl":"https://doi.org/10.2147/ANTI.S39718","url":null,"abstract":"Serologic assays detecting antibodies to Borrelia burgdorferi are useful in the routine diagnosis of Lyme disease. Despite the presence of new and improved assays, current laboratory diagnosis still requires optimization. The variety of genospecies and their different geographic distributions are the reasons why standards and recommendations are not the same for all of the main geographic regions, ie, USA, Asia, and Europe. Moreover, the variety and variability of antigens represents a significant challenge in assay design. This is due to the various antigens among the genospecies responsible for Lyme borreliosis; the changing antigens presented during infection; and the variability of single antigens. This review article discusses the immunologic response in Lyme disease over time, and the advantages and disadvantages of existing serological tests. Two tier testing is also introduced. Antigens useful for diagnosis, the properties of individual antigens and their appearance in infection especially the antigens appearing during mammalian infection, so-called “in vivo” antigens are introduced. To determine antibodies confirming infection in the nervous system, the same restrictions with regard to interpretation of enzyme-linked immunosorbent assay results in serum apply to cerebrospinal fluid. Furthermore, concentrations of antibodies in the two compartments, ie, blood and cerebrospinal fluid, are variable depending on compartmentalization (anatomic sequestration) and immunologic phenomena at immunologically privileged sites, such as the intrathecal space. To confirm neuroborreliosis, synthesis of antibodies in cerebrospinal fluid, should be measured in the form of a so-called antibody index. Further studies should focus on detecting the lowest concentration of antibodies and looking for useful new antigens, and the relationship between composition of such antigens and the patient’s clinical status.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"126 1","pages":"33-44"},"PeriodicalIF":0.0,"publicationDate":"2014-07-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S39718","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302271","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}
L. Blohm, C. Püttmann, Simone Holz, G. Piechotta, J. Albers, C. Dammers, M. Kleines, A. Krüttgen, G. Melmer, J. Nähring, S. Barth, E. Nebling
The detection of hepatitis C virus (HCV) in the blood of patients is currently based on immunological assays (enzyme-linked immunosorbent assay (ELISA) and recombinant immunoblot assay) that use different HCV epitopes to detect anti-HCV antibodies, and these tests usually require laboratories and trained personnel. The ELISA-based systems are also time consuming. Portable diagnostic devices offering rapid test results would therefore be advanta- geous in the field of medical care. To facilitate the fast and reliable diagnosis of HCV, we used a miniaturized automated system based on a cartridge with an integrated electrical biochip for the decentralized detection of anti-HCV antibodies against the Core, NS3, and NS4A proteins. This system allows the detection of virus-specific antibodies in 2 µL of serum or whole blood within 15 minutes using an ELISA directly on a gold electrode array containing HCV proteins as the capture antigen. The sensitivity of this system is comparable with standard microtiter plate ELISAs, but the duration of the novel assay is 5%-6% that of standard ELISAs.
{"title":"rapid detection of different human anti-hcV immunoglobulins on electrical biochips","authors":"L. Blohm, C. Püttmann, Simone Holz, G. Piechotta, J. Albers, C. Dammers, M. Kleines, A. Krüttgen, G. Melmer, J. Nähring, S. Barth, E. Nebling","doi":"10.2147/ANTI.S54763","DOIUrl":"https://doi.org/10.2147/ANTI.S54763","url":null,"abstract":"The detection of hepatitis C virus (HCV) in the blood of patients is currently based on immunological assays (enzyme-linked immunosorbent assay (ELISA) and recombinant immunoblot assay) that use different HCV epitopes to detect anti-HCV antibodies, and these tests usually require laboratories and trained personnel. The ELISA-based systems are also time consuming. Portable diagnostic devices offering rapid test results would therefore be advanta- geous in the field of medical care. To facilitate the fast and reliable diagnosis of HCV, we used a miniaturized automated system based on a cartridge with an integrated electrical biochip for the decentralized detection of anti-HCV antibodies against the Core, NS3, and NS4A proteins. This system allows the detection of virus-specific antibodies in 2 µL of serum or whole blood within 15 minutes using an ELISA directly on a gold electrode array containing HCV proteins as the capture antigen. The sensitivity of this system is comparable with standard microtiter plate ELISAs, but the duration of the novel assay is 5%-6% that of standard ELISAs.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"4 1","pages":"23-32"},"PeriodicalIF":0.0,"publicationDate":"2014-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S54763","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302687","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}
A. Lathrop, Taylor W. Bailey, Kwang-Pyo Kim, A. Bhunia
: Listeria monocytogenes continues to be a major public health risk and there is a need for improved rapid detection methods. New and highly specific L. monocytogenes antibodies are needed to advance current detection and meet the needs of industry. This research compared the L. monocytogenes genome with that of L. innocua (a nonpathogenic species of Listeria ) and identified nine surface proteins specific to L. monocytogenes . Protein sequences were collected from the database and properties such as hydropathy profile and transmembrane topology were analyzed using TMpred software. Nine peptide sequences were chosen, and synthetic peptides were made and administered to rabbits for antibody production. All nine antibodies were screened against a panel of L. monocytogenes , nonpathogenic Listeria , and non-Listeria bacteria. Two of the nine antibodies, ie, the Lm404 and LmC639 polyclonal antibodies, showed a specific reaction to L. monocytogenes internalin B and actin polymerization protein, respectively, and were characterized further by enzyme-linked immunosorbent assay, Western blot, and transmission electron microscopy. In Western blot, both antibodies reacted with the targeted protein and did not cross-react with other Listeria spp. The Lm404 polyclonal antibody showed a high reaction with the panel of 41 L. monocytogenes strains while the LmC639 polyclonal antibody showed a weak reaction. Both the Lm404 and LmC639 polyclonal antibodies showed potential for use in immunoassays for specific detection of L. monocytogenes . This study further indicates that comparative genomics could be used to select pathogen-specific antigen for antibody production.
{"title":"Pathogen-specific antigen target for production of antibodies produced by comparative genomics","authors":"A. Lathrop, Taylor W. Bailey, Kwang-Pyo Kim, A. Bhunia","doi":"10.2147/ANTI.S54848","DOIUrl":"https://doi.org/10.2147/ANTI.S54848","url":null,"abstract":": Listeria monocytogenes continues to be a major public health risk and there is a need for improved rapid detection methods. New and highly specific L. monocytogenes antibodies are needed to advance current detection and meet the needs of industry. This research compared the L. monocytogenes genome with that of L. innocua (a nonpathogenic species of Listeria ) and identified nine surface proteins specific to L. monocytogenes . Protein sequences were collected from the database and properties such as hydropathy profile and transmembrane topology were analyzed using TMpred software. Nine peptide sequences were chosen, and synthetic peptides were made and administered to rabbits for antibody production. All nine antibodies were screened against a panel of L. monocytogenes , nonpathogenic Listeria , and non-Listeria bacteria. Two of the nine antibodies, ie, the Lm404 and LmC639 polyclonal antibodies, showed a specific reaction to L. monocytogenes internalin B and actin polymerization protein, respectively, and were characterized further by enzyme-linked immunosorbent assay, Western blot, and transmission electron microscopy. In Western blot, both antibodies reacted with the targeted protein and did not cross-react with other Listeria spp. The Lm404 polyclonal antibody showed a high reaction with the panel of 41 L. monocytogenes strains while the LmC639 polyclonal antibody showed a weak reaction. Both the Lm404 and LmC639 polyclonal antibodies showed potential for use in immunoassays for specific detection of L. monocytogenes . This study further indicates that comparative genomics could be used to select pathogen-specific antigen for antibody production.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"4 1","pages":"13-22"},"PeriodicalIF":0.0,"publicationDate":"2014-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S54848","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302838","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}
License. The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. Permissions beyond the scope of the License are administered by Dove Medical Press Limited. Information on how to request permission may be found at: http://www.dovepress.com/permissions.php Antibody Technology Journal 2014:4 1–12 Antibody Technology Journal Dovepress
{"title":"Monoclonal antibodies for the prevention of rabies: theory and clinical practice","authors":"T. Nagarajan, W. Marissen, Charles E. Rupprecht","doi":"10.2147/ANTI.S33533","DOIUrl":"https://doi.org/10.2147/ANTI.S33533","url":null,"abstract":"License. The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. Permissions beyond the scope of the License are administered by Dove Medical Press Limited. Information on how to request permission may be found at: http://www.dovepress.com/permissions.php Antibody Technology Journal 2014:4 1–12 Antibody Technology Journal Dovepress","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"4 1","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"2014-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S33533","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302655","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}
In light of recent developments in the production of human monoclonal antibodies, particularly the method based on isolation of immunoglobulin genes from antigen-specific B cells, the hybridoma technology has become obsolete to some extent. However, the method requires a relatively simple procedure at a low cost and has inherently valuable features, includ- ing continuous production of the whole molecule of specific antibodies that retain their native structure. Furthermore, several technical improvements, including accessibility to a panel of various partner cells, enhanced Epstein-Barr virus transformation and optimized electroporation, have increased the fusion efficiency for production of hybrids. Finally, a hybridoma-produced monoclonal antibody (mAb) can be used to test whether certain functions of a recombinant mAb, produced by molecular techniques from the same clone of B cells, correspond to the native antibodies. Access to several different methods of mAb production, including hybridoma technology, potentiates our capability to understand the human immune response to various invading pathogens and tumors with the perspective of using the antibodies for diagnosis and
{"title":"Human hybridoma technology","authors":"M. Gorny","doi":"10.2147/ANTI.S30489","DOIUrl":"https://doi.org/10.2147/ANTI.S30489","url":null,"abstract":"In light of recent developments in the production of human monoclonal antibodies, particularly the method based on isolation of immunoglobulin genes from antigen-specific B cells, the hybridoma technology has become obsolete to some extent. However, the method requires a relatively simple procedure at a low cost and has inherently valuable features, includ- ing continuous production of the whole molecule of specific antibodies that retain their native structure. Furthermore, several technical improvements, including accessibility to a panel of various partner cells, enhanced Epstein-Barr virus transformation and optimized electroporation, have increased the fusion efficiency for production of hybrids. Finally, a hybridoma-produced monoclonal antibody (mAb) can be used to test whether certain functions of a recombinant mAb, produced by molecular techniques from the same clone of B cells, correspond to the native antibodies. Access to several different methods of mAb production, including hybridoma technology, potentiates our capability to understand the human immune response to various invading pathogens and tumors with the perspective of using the antibodies for diagnosis and","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"2 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2012-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S30489","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302587","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}
: Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.
{"title":"Detection of in situ cleaved p115 with the cut specific antibodies in rapid protein inactivation system by tobacco etch viral protease cleavage","authors":"Mayuko Koreishi, Yasuko Honjo, Ayano Satoh","doi":"10.2147/ANTI.S22825","DOIUrl":"https://doi.org/10.2147/ANTI.S22825","url":null,"abstract":": Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"1 1","pages":"5-11"},"PeriodicalIF":0.0,"publicationDate":"2011-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S22825","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68302479","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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