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
Open accessAbstract
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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“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.”
From Intestinal microbiota signatures of clinical response and immune-related adverse events in melanoma patients treated with anti-PD-1 (2022) · cites this paper as [57]
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Raetz, C. R. H., & Whitfield, C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135414 · Cited by 4,404
Acinetobacter baumannii : Emergence of a Successful Pathogen
Peleg, A. Y., Seifert, H., & Paterson, D. L. (2008) · Clinical Microbiology Reviews · doi:10.1128/cmr.00058-07 · Cited by 3,416
Westphal, O. (1965) · Medical Entomology and Zoology · Cited by 2,533
The Epidemiology and Control of Acinetobacter baumannii in Health Care Facilities
Fournier, P., Richet, H., & Weinstein, R. A. (2006) · Clinical Infectious Diseases · doi:10.1086/500202 · Cited by 995
Maragakis, L. L., & Perl, T. M. (2008) · Clinical Infectious Diseases · doi:10.1086/529198 · Cited by 972
Comparative Genome Sequence Analysis of Multidrug-Resistant Acinetobacter baumannii
Adams, M. D., Goglin, K. C., Molyneaux, N., Hujer, K. M., Lavender, H. F., Jamison, J. J., MacDonald, I. J., Martin, K. M., Russo, T. A., Campagnari, A. A., et al. (2008) · Journal of Bacteriology · doi:10.1128/jb.00834-08 · Cited by 434
Self-citationScott, P. T., Deye, G. A., Srinivasan, A., Murray, C. K., Moran, K., Hulten, E. A., Fishbain, J. T., Craft, D. W., Riddell, S. W., Lindler, L., et al. (2007) · Clinical Infectious Diseases · doi:10.1086/518170 · Cited by 391
Multidrug-ResistantAcinetobacterExtremity Infections in Soldiers
Davis, K. A., Moran, K. A., McAllister, C. K., & Gray, P. J. (2005) · Emerging infectious diseases · doi:10.3201/1108.050103 · Cited by 327
Identification and Characterization of an Acinetobacter baumannii Biofilm-Associated Protein
Loehfelm, T. W., Luke, N. R., & Campagnari, A. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.01416-07 · Cited by 283
Self-citationPier, G. B. (2007) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2007.03.012 · Cited by 258
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Acinetobacter baumannii Antibiotic Resistance Mechanisms
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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
- Publisher
- American Society for Microbiology
- Published
- 2010-05
- Volume
- 78
- Issue
- 5
- Pages
- 2017-2023
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC2863528
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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