Collagen Binding Proteins of Gram-Positive Pathogens

Collagens are the primary structural components of mammalian extracellular matrices. In addition, collagens regulate tissue development, regeneration and host defense through interaction with specific cellular receptors. Their unique triple helix structure, which requires a glycine residue every thi...

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Main Authors: Srishtee Arora, Jay Gordon, Magnus Hook
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-02-01
Series:Frontiers in Microbiology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmicb.2021.628798/full
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author Srishtee Arora
Jay Gordon
Magnus Hook
author_facet Srishtee Arora
Jay Gordon
Magnus Hook
author_sort Srishtee Arora
collection DOAJ
description Collagens are the primary structural components of mammalian extracellular matrices. In addition, collagens regulate tissue development, regeneration and host defense through interaction with specific cellular receptors. Their unique triple helix structure, which requires a glycine residue every third amino acid, is the defining structural feature of collagens. There are 28 genetically distinct collagens in humans. In addition, several other unrelated human proteins contain a collagen domain. Gram-positive bacteria of the genera Staphylococcus, Streptococcus, Enterococcus, and Bacillus express cell surface proteins that bind to collagen. These proteins of Gram-positive pathogens are modular proteins that can be classified into different structural families. This review will focus on the different structural families of collagen binding proteins of Gram-positive pathogen. We will describe how these proteins interact with the triple helix in collagens and other host proteins containing a collagenous domain and discuss how these interactions can contribute to the pathogenic processes.
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spelling doaj.art-5ff1bafe7a354a6495c1f644541903382022-12-21T19:58:51ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-02-011210.3389/fmicb.2021.628798628798Collagen Binding Proteins of Gram-Positive PathogensSrishtee AroraJay GordonMagnus HookCollagens are the primary structural components of mammalian extracellular matrices. In addition, collagens regulate tissue development, regeneration and host defense through interaction with specific cellular receptors. Their unique triple helix structure, which requires a glycine residue every third amino acid, is the defining structural feature of collagens. There are 28 genetically distinct collagens in humans. In addition, several other unrelated human proteins contain a collagen domain. Gram-positive bacteria of the genera Staphylococcus, Streptococcus, Enterococcus, and Bacillus express cell surface proteins that bind to collagen. These proteins of Gram-positive pathogens are modular proteins that can be classified into different structural families. This review will focus on the different structural families of collagen binding proteins of Gram-positive pathogen. We will describe how these proteins interact with the triple helix in collagens and other host proteins containing a collagenous domain and discuss how these interactions can contribute to the pathogenic processes.https://www.frontiersin.org/articles/10.3389/fmicb.2021.628798/fullGram-positive bacteriacollagen binding proteinscollagen-like proteinssurface proteinscollagen
spellingShingle Srishtee Arora
Jay Gordon
Magnus Hook
Collagen Binding Proteins of Gram-Positive Pathogens
Frontiers in Microbiology
Gram-positive bacteria
collagen binding proteins
collagen-like proteins
surface proteins
collagen
title Collagen Binding Proteins of Gram-Positive Pathogens
title_full Collagen Binding Proteins of Gram-Positive Pathogens
title_fullStr Collagen Binding Proteins of Gram-Positive Pathogens
title_full_unstemmed Collagen Binding Proteins of Gram-Positive Pathogens
title_short Collagen Binding Proteins of Gram-Positive Pathogens
title_sort collagen binding proteins of gram positive pathogens
topic Gram-positive bacteria
collagen binding proteins
collagen-like proteins
surface proteins
collagen
url https://www.frontiersin.org/articles/10.3389/fmicb.2021.628798/full
work_keys_str_mv AT srishteearora collagenbindingproteinsofgrampositivepathogens
AT jaygordon collagenbindingproteinsofgrampositivepathogens
AT magnushook collagenbindingproteinsofgrampositivepathogens