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Author
- Bensing, Barbara A1
- Carlson, Russell W1
- Chen, Yu1
- Dobruchowska, Justyna M1
- Feldman, Mario F1
- Jeffrey, Philip D1
- Liao, Maofu1
- Melville, Stephen B1
- Mi, Wei1
- Mills, Dominic C1
- Nation, Patrick1
- Nothaft, Harald1
- Rapoport, Tom A1
- Seepersaud, Ravin1
- Shajahan, Asif1
- Sonon, Roberto N1
- Sullam, Paul M1
- Szymanski, Christine M1
- Vlach, Jiri1
- Wenzel, Cory Q1
Keyword
- adhesin1
- bacterial pathogenesis1
- carbohydrate biosynthesis1
- carbohydrate structure1
- cell surface1
- cell wall1
- Clostridium perfringens1
- crystallography1
- food safety1
- foodborne illness1
- glycobiology1
- glycoconjugate1
- glycoconjugate vaccines1
- glycolipid structure1
- glycosylation1
- glycosyltransferase1
- Gram-positive bacteria1
- lipoteichoic acid (LTA)1
- microbial pathogenesis1
- microbiology1
- necrotic enteritis1
- NMR spectroscopy1
- one health1
- protein export1
- protein secretion1
Microbiology
2 Results
- Glycobiology and Extracellular MatricesOpen Access
An atypical lipoteichoic acid from Clostridium perfringens elicits a broadly cross-reactive and protective immune response
Journal of Biological ChemistryVol. 295Issue 28p9513–9530Published online: May 18, 2020- Cory Q. Wenzel
- Dominic C. Mills
- Justyna M. Dobruchowska
- Jiri Vlach
- Harald Nothaft
- Patrick Nation
- and others
Cited in Scopus: 9Clostridium perfringens is a leading cause of food-poisoning and causes avian necrotic enteritis, posing a significant problem to both the poultry industry and human health. No effective vaccine against C. perfringens is currently available. Using an antiserum screen of mutants generated from a C. perfringens transposon-mutant library, here we identified an immunoreactive antigen that was lost in a putative glycosyltransferase mutant, suggesting that this antigen is likely a glycoconjugate. Following injection of formalin-fixed whole cells of C. - Editors' PicksOpen Access
Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii
Journal of Biological ChemistryVol. 293Issue 14p5360–5373Published online: February 9, 2018- Yu Chen
- Barbara A. Bensing
- Ravin Seepersaud
- Wei Mi
- Maofu Liao
- Philip D. Jeffrey
- and others
Cited in Scopus: 13Many pathogenic bacteria, including Streptococcus gordonii, possess a pathway for the cellular export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. This adhesin protein is O-glycosylated by several cytosolic glycosyltransferases and requires three accessory Sec proteins (Asp1–3) for export, but how the adhesin protein is processed for export is not well understood. Here, we report that the S. gordonii adhesin GspB is sequentially O-glycosylated by three enzymes (GtfA/B, Nss, and Gly) that attach N-acetylglucosamine and glucose to Ser/Thr residues.