Subversion of a family of antimicrobial proteins by Salmonella enterica
Salmonella enterica is a food-borne pathogen able to cause a wide spectrum of diseases ranging from mild gastroenteritis to systemic infections. During almost all stages of the infection process Salmonella is likely to be exposed to a wide variety of host-derived antimicrobial peptides (AMPs). AM...
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Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Philipps-Universität Marburg
2024
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Subjects: | |
Online Access: | PDF Full Text |
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Summary: | Salmonella enterica is a food-borne pathogen able to cause a wide spectrum of
diseases ranging from mild gastroenteritis to systemic infections. During almost
all stages of the infection process Salmonella is likely to be exposed to a wide
variety of host-derived antimicrobial peptides (AMPs). AMPs are important
components of the innate immune response which integrate within the
bacterial membrane, thus forming pores which lead ultimately to bacterial
killing. In contrast to other AMPs Bactericidal/Permeability-increasing Protein
(BPI) displayed only weak bacteriostatic or bactericidal effects towards
Salmonella enterica sv. Typhimurium (STM) cultures. Surprisingly, we found
that sub-antimicrobial concentrations of BPI fold-containing (BPIF) superfamily
members mediated adhesion of STM depending on pre-formed type 1 fimbriae.
BPIF proteins directly bind to type 1 fimbriae through mannose-containing
oligosaccharide modifications. Fimbriae decorated with BPIF proteins exhibit
extended binding specificity, allowing for bacterial adhesion on a greater variety
of abiotic and biotic surfaces likely promoting host colonization. Further, fimbriae
significantly contributed to the resistance against BPI, probably through
sequestration of the AMP before membrane interaction. In conclusion,
functional subversion of innate immune proteins of the BPIF family through
binding to fimbriae promotes Salmonella virulence by survival of host defense
and promotion of host colonization. |
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Item Description: | Gefördert durch den Open-Access-Publikationsfonds der UB Marburg. |
DOI: | 10.3389/fcimb.2024.1375887 |