Production of Recombinant Polypeptides Containing One GA-Module and Analysis of Their Ability to Bind to Human Albumin
Surface proteins of many bacterial species interact with human serum albumin (HSA) via a special region of amino acid sequence termed GA module. For instance, surface peptostreptococcal albumin-binding protein of anaerobic bacteria Peptostreptococcus magnus contains one HSA-binding GA-module. Protei...
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Published in | Bulletin of experimental biology and medicine Vol. 162; no. 1; pp. 66 - 70 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
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Springer US
01.11.2016
Springer Springer Nature B.V |
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Abstract | Surface proteins of many bacterial species interact with human serum albumin (HSA) via a special region of amino acid sequence termed GA module. For instance, surface peptostreptococcal albumin-binding protein of anaerobic bacteria
Peptostreptococcus magnus
contains one HSA-binding GA-module. Protein G from group G and C
Streptococcus
strains isolated from humans has HSA-binding region consisting of three GA-modules. HSA-binding protein containing two GA-modules was found in strains of group G
Streptococcus
of animal origin. We obtained two recombinant polypeptides GA1 and GA2 congaing one GA-module each. Recombinant polypeptide with two GA-modules binds HSA with a much higher affinity than polypeptides GA1 and GA2 containing one GA-module. Polypeptide with the second GAmodule more effectively binds HSA than polypeptides with the GA-module. |
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AbstractList | Surface proteins of many bacterial species interact with human serum albumin (HSA) via a special region of amino acid sequence termed GA module. For instance, surface peptostreptococcal albumin-binding protein of anaerobic bacteria Peptostreptococcus magnus contains one HSA-binding GA-module. Protein G from group G and C Streptococcus strains isolated from humans has HSA-binding region consisting of three GA-modules. HSA-binding protein containing two GA-modules was found in strains of group G Streptococcus of animal origin. We obtained two recombinant polypeptides GA1 and GA2 congaing one GA-module each. Recombinant polypeptide with two GA-modules binds HSA with a much higher affinity than polypeptides GA1 and GA2 containing one GA-module. Polypeptide with the second GAmodule more effectively binds HSA than polypeptides with the GA-module. Surface proteins of many bacterial species interact with human serum albumin (HSA) via a special region of amino acid sequence termed GA module. For instance, surface peptostreptococcal albumin-binding protein of anaerobic bacteria Peptostreptococcus magnus contains one HSA-binding GA-module. Protein G from group G and C Streptococcus strains isolated from humans has HSA-binding region consisting of three GA-modules. HSA-binding protein containing two GA-modules was found in strains of group G Streptococcus of animal origin. We obtained two recombinant polypeptides GA1 and GA2 congaing one GA-module each. Recombinant polypeptide with two GA-modules binds HSA with a much higher affinity than polypeptides GA1 and GA2 containing one GA-module. Polypeptide with the second GAmodule more effectively binds HSA than polypeptides with the GA-module. Key Words: Streptococcus group G; human serum albumin binding polypeptide; GA-module Surface proteins of many bacterial species interact with human serum albumin (HSA) via a special region of amino acid sequence termed GA module. For instance, surface peptostreptococcal albumin-binding protein of anaerobic bacteria Peptostreptococcus magnus contains one HSA-binding GA-module. Protein G from group G and C Streptococcus strains isolated from humans has HSA-binding region consisting of three GA-modules. HSA-binding protein containing two GA-modules was found in strains of group G Streptococcus of animal origin. We obtained two recombinant polypeptides GA1 and GA2 congaing one GA-module each. Recombinant polypeptide with two GA-modules binds HSA with a much higher affinity than polypeptides GA1 and GA2 containing one GA-module. Polypeptide with the second GAmodule more effectively binds HSA than polypeptides with the GA-module. |
Audience | Academic |
Author | Gupalova, T. V. Bormotova, E. A. |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27878724$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1016/0003-2697(87)90587-2 10.1007/s10517-015-2972-z 10.17686/sced_rusnauka_2012-1640 10.1128/MMBR.63.1.174-229.1999 10.1016/S0021-9258(17)32693-5 10.1128/IAI.60.9.3601-3608.1992 |
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Keywords | GA-module human serum albumin binding polypeptide Streptococcus group G |
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References | Bormotova, Gupalova (CR1) 2015; 159 Navarre, Schneewind (CR8) 1999; 63 CR2 Schägger, von Jagow (CR9) 1987; 166 CR4 CR6 CR5 Sjöbring (CR10) 1992; 60 Gupalova, Bormotova, Gladilina, Totolyan (CR3) 2012; 3 de Château, Björck (CR7) 1994; 269 EA Bormotova (3547_CR1) 2015; 159 WW Navarre (3547_CR8) 1999; 63 TV Gupalova (3547_CR3) 2012; 3 3547_CR6 3547_CR5 3547_CR2 U Sjöbring (3547_CR10) 1992; 60 3547_CR4 M Château de (3547_CR7) 1994; 269 H Schägger (3547_CR9) 1987; 166 |
References_xml | – volume: 166 start-page: 368 issue: 2 year: 1987 end-page: 379 ident: CR9 article-title: Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90587-2 contributor: fullname: von Jagow – volume: 60 start-page: 3601 issue: 9 year: 1992 end-page: 3608 ident: CR10 article-title: Isolation and molecular characterization of a novel albumin-binding protein from group G streptococci publication-title: Infect. Immun. contributor: fullname: Sjöbring – ident: CR6 – volume: 63 start-page: 174 issue: 1 year: 1999 end-page: 229 ident: CR8 article-title: Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope publication-title: Microbiol. Mol. Biol. Rev. contributor: fullname: Schneewind – ident: CR5 – volume: 159 start-page: 393 issue: 3 year: 2015 end-page: 397 ident: CR1 article-title: The relationship between albumin-binding capacity of recombinant polypeptide and changes in the structure of albumin-binding domain publication-title: Bull. Exp. Biol. Med. doi: 10.1007/s10517-015-2972-z contributor: fullname: Gupalova – ident: CR4 – ident: CR2 – volume: 3 start-page: 75 year: 2012 end-page: 84 ident: CR3 article-title: Preparation and characterization of recombinant albumin-binding polypeptide of group G Streptococcus for the diagnosis of diabetic nephropathy publication-title: Biotekhnologiya. doi: 10.17686/sced_rusnauka_2012-1640 contributor: fullname: Totolyan – volume: 269 start-page: 12,147 issue: 16 year: 1994 end-page: 12,151 ident: CR7 article-title: Protein PAB, a mosaic albumin-binding bacterial protein representing the fi rst contemporary example of module shuffling publication-title: J. Biol. Chem contributor: fullname: Björck – ident: 3547_CR2 – volume: 63 start-page: 174 issue: 1 year: 1999 ident: 3547_CR8 publication-title: Microbiol. Mol. Biol. Rev. doi: 10.1128/MMBR.63.1.174-229.1999 contributor: fullname: WW Navarre – volume: 166 start-page: 368 issue: 2 year: 1987 ident: 3547_CR9 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90587-2 contributor: fullname: H Schägger – ident: 3547_CR4 – ident: 3547_CR6 – volume: 159 start-page: 393 issue: 3 year: 2015 ident: 3547_CR1 publication-title: Bull. Exp. Biol. Med. doi: 10.1007/s10517-015-2972-z contributor: fullname: EA Bormotova – volume: 3 start-page: 75 year: 2012 ident: 3547_CR3 publication-title: Biotekhnologiya. doi: 10.17686/sced_rusnauka_2012-1640 contributor: fullname: TV Gupalova – ident: 3547_CR5 – volume: 269 start-page: 12,147 issue: 16 year: 1994 ident: 3547_CR7 publication-title: J. Biol. Chem doi: 10.1016/S0021-9258(17)32693-5 contributor: fullname: M Château de – volume: 60 start-page: 3601 issue: 9 year: 1992 ident: 3547_CR10 publication-title: Infect. Immun. doi: 10.1128/IAI.60.9.3601-3608.1992 contributor: fullname: U Sjöbring |
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SubjectTerms | Albumin Amino Acid Sequence Amino acids Anaerobic bacteria Bacterial Proteins - biosynthesis Bacterial Proteins - chemistry Bacterial Proteins - genetics Base Sequence Binding Sites Biomedical and Life Sciences Biomedicine Cell Biology Cloning, Molecular Escherichia coli - chemistry Escherichia coli - genetics Gene Expression Human serum albumin Humans Internal Medicine Laboratory Medicine Pathology Peptostreptococcus magnus Polypeptides Protein Binding Protein G Protein Interaction Domains and Motifs Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics Serum Albumin - chemistry Solutions Strains (organisms) Streptococcus Streptococcus - chemistry Streptococcus - genetics |
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Title | Production of Recombinant Polypeptides Containing One GA-Module and Analysis of Their Ability to Bind to Human Albumin |
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