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 inBulletin of experimental biology and medicine Vol. 162; no. 1; pp. 66 - 70
Main Authors Bormotova, E. A., Gupalova, T. V.
Format Journal Article
LanguageEnglish
Published New York 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.
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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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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Snippet 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,...
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StartPage 66
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
URI https://link.springer.com/article/10.1007/s10517-016-3547-3
https://www.ncbi.nlm.nih.gov/pubmed/27878724
https://www.proquest.com/docview/1860898775/abstract/
https://search.proquest.com/docview/1843921750
https://search.proquest.com/docview/1868333584
Volume 162
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