Cited by 114Antibiotic Resistance in BacteriaBacterial Genetics and BiotechnologyBacterial Infections and Vaccines

The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.

Identification and Characterization of a Glycosyltransferase Involved in Acinetobacter baumannii Lipopolysaccharide Core Biosynthesis

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Abstract

Although Acinetobacter baumannii has emerged as a significant cause of nosocomial infections worldwide, there have been few investigations describing the factors important for A. baumannii persistence and pathogenesis. This paper describes the first reported identification of a glycosyltransferase, LpsB, involved in lipopolysaccharide (LPS) biosynthesis in A. baumannii . Mutational, structural, and complementation analyses indicated that LpsB is a core oligosaccharide glycosyl transferase. Using a genetic approach, lpsB was compared with the lpsB homologues of several A. baumannii strains. These analyses indicated that LpsB is highly conserved among A. baumannii isolates. Furthermore, we developed a monoclonal antibody, monoclonal antibody 13C11, which reacts to an LPS core epitope expressed by approximately one-third of the A. baumannii clinical isolates evaluated to date. Previous studies describing the heterogeneity of A. baumannii LPS were limited primarily to structural analyses; therefore, studies evaluating the correlation between these surface glycolipids and pathogenesis were warranted. Our data from an evaluation of LpsB mutant 307::TN17, which expresses a deeply truncated LPS glycoform consisting of only two 3-deoxy- d -manno-octulosonic acid residues and lipid A, suggest that A. baumannii LPS is important for resistance to normal human serum and confers a competitive advantage for survival in vivo . These results have important implications for the role of LPS in A. baumannii infections.

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Crossref · 10.1128/iai.00016-10

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  • Bacterial genes for alpha-l-fucosidase, alpha-galactosidase and glycosyltransferases were enriched in non-responders.

    “Using a new binning approach to focus on candidate bacterial driver genes, we observed enrichment of bacterial genes encoding key enzymes: polysaccharide deacetylase (associated with reduction of polysaccharide immunogenicity42) in Rs; and alpha-l-fucosidase45 and alpha-galactosidase46 (associated with mucus degradation) and glycosyltransferases (associated with LPS synthesis57) in NRs.”

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Metadata

Authors
Luke, N. R., Sauberan, S. L., Russo, T. A., Beanan, J. M., Olson, R., Loehfelm, T. W., Cox, A. D., St. Michael, F., Vinogradov, E. V., & Campagnari, A. A.
Affiliations
  • Department of Microbiology
  • VA Western New York Healthcare System (US)
  • University at Buffalo, State University of New York (US)
  • Institute for Biological Sciences (CA)
  • Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A 0R6
Corresponding author
Campagnari, Anthony A.
Venue
Infection and Immunity
Published
2010-05
Volume
78
Issue
5
Pages
2017-2023
ISSN
  • 0019-9567 (ISSN-L)
  • 1098-5522
OpenAlex
W2118531873
Cited by
114
References
45
Citations by year
2026: 5 · 2025: 9 · 2024: 9 · 2023: 8 · 2022: 7 · 2021: 9 · 2020: 6 · 2019: 6 · 2018: 7 · 2017: 5 · 2016: 7 · 2015: 8 · 2014: 7 · 2013: 6 · 2012: 8
FWCI
3.14
Type
journal article
Language
en
Open access
Locations
  • Infection and Immunity (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • NPARC (submittedVersion)
Funders
National Research Council Canada
Topics
  • Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
Keywords
Acinetobacter baumannii, LPS core oligosaccharide, 3-deoxy-D-manno-octulosonic acid, lipid A, human serum resistance, bacterial pathogenesis, nosocomial infections
MeSH terms
Acinetobacter Infections, Animals, Bacterial Proteins, Blood Bactericidal Activity, Genetic Complementation Test, Humans, Lipopolysaccharides, Mice, Inbred BALB C, Colony Count, Microbial, Mutagenesis, Insertional, Glycosyltransferases, Conserved Sequence, Sequence Homology, Amino Acid, Soft Tissue Infections, Acinetobacter baumannii, Microbial Viability, Mice, Rats, Gene Knockout Techniques

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