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Author
- Carlson, Russell W2
- Ambiel, Ina1
- Bensing, Barbara A1
- Chen, Yu1
- Crocker, Paul R1
- Dobruchowska, Justyna M1
- Erikson, Elina1
- Feldman, Mario F1
- Frank, Martin1
- Heiss, Christian1
- Hjuler, Christian T1
- Izquierdo-Useros, Nuria1
- Jeffrey, Philip D1
- Kelly, Simon J1
- Keppler, Oliver T1
- Liao, Maofu1
- Martinez-Picado, Javier1
- Meier, Chris1
- Melville, Stephen B1
- Mi, Wei1
- Mills, Dominic C1
- Muszyński, Artur1
- Nation, Patrick1
- Nothaft, Harald1
Keyword
- carbohydrate structure2
- glycobiology2
- glycoconjugate2
- acetylation1
- adhesin1
- bacterial pathogenesis1
- carbohydrate biosynthesis1
- cell surface1
- cell wall1
- Clostridium perfringens1
- crystallography1
- exopolysaccharide1
- food safety1
- foodborne illness1
- glycoconjugate vaccines1
- glycolipid structure1
- glycosylation1
- glycosyltransferase1
- Gram-positive bacteria1
- infectious disease1
- lipoteichoic acid (LTA)1
- Mesorhizobium loti1
- microbial pathogenesis1
- microbiology1
- NMR spectroscopy1
Microbiology
4 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. - Glycobiology and Extracellular MatricesOpen Access
Structures of Exopolysaccharides Involved in Receptor-mediated Perception of Mesorhizobium loti by Lotus japonicus
Journal of Biological ChemistryVol. 291Issue 40p20946–20961Published online: September 1, 2016- Artur Muszyński
- Christian Heiss
- Christian T. Hjuler
- John T. Sullivan
- Simon J. Kelly
- Mikkel B. Thygesen
- and others
Cited in Scopus: 26In the symbiosis formed between Mesorhizobium loti strain R7A and Lotus japonicus Gifu, rhizobial exopolysaccharide (EPS) plays an important role in infection thread formation. Mutants of strain R7A affected in early exopolysaccharide biosynthetic steps form nitrogen-fixing nodules on L. japonicus Gifu after a delay, whereas mutants affected in mid or late biosynthetic steps induce uninfected nodule primordia. Recently, it was shown that a plant receptor-like kinase, EPR3, binds low molecular mass exopolysaccharide from strain R7A to regulate bacterial passage through the plant's epidermal cell layer (Kawaharada, Y., Kelly, S., Nielsen, M. - Glycobiology and Extracellular MatricesOpen Access
Mouse Siglec-1 Mediates trans-Infection of Surface-bound Murine Leukemia Virus in a Sialic Acid N-Acyl Side Chain-dependent Manner
Journal of Biological ChemistryVol. 290Issue 45p27345–27359Published online: September 14, 2015- Elina Erikson
- Paul R. Wratil
- Martin Frank
- Ina Ambiel
- Katharina Pahnke
- Maria Pino
- and others
Cited in Scopus: 31Background: Human Siglec-1 mediates HIV trans-infection by interaction with virion-associated sialylated gangliosides.Results: Here, Siglec-1 on mouse macrophages mediated trans-infection of surface-bound MLV. This could be inhibited by biosynthetic modification of sialic acids' N-acyl side chain in virus-producer cells.Conclusion: The N-acyl side chain is a critical determinant of Siglec-1-dependent MLV trans-infection.Significance: Glycoengineering allows manipulation of sialic acid-dependent virus/receptor interactions.