The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Resistance to host antimicrobial peptides is necessary for Salmonella virulence.
Open accessAbstract
The production of antibacterial peptides is a host defense strategy used by various species, including mammals, amphibians, and insects. Successful pathogens, such as the facultative intracellular bacterium Salmonella typhimurium, have evolved resistance mechanisms to this ubiquitous type of host defense. To identify the genes required for resistance to host peptides, we isolated a library of 20,000 MudJ transposon insertion mutants of a virulent peptide-resistant S. typhimurium strain and screened it for hypersensitivity to the antimicrobial peptide protamine. Eighteen mutants had heightened susceptibility to protamine and 12 of them were characterized in detail. Eleven mutants were attenuated for virulence in vivo when inoculated into BALB/c mice by the intragastric route, and 8 of them were also avirulent following intraperitoneal inoculation. The mutants fell into different phenotypic classes with respect to their susceptibility to rabbit defensin NP-1, frog magainin 2, pig cecropin P1, and the insect venom-derived peptides mastoparan and melittin. The resistance loci mapped to eight distinct locations in the genome. Characterization of the mutants showed that one had a defective lipopolysaccharide and another mutant harbored a mutation in phoP, a locus previously shown to control expression of Salmonella virulence genes. Our data indicate that the ability to resist the killing effect of host antimicrobial peptides is a virulence property and that several resistance mechanisms operate in S. typhimurium.
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Benjamin, W. H., Hall, P., & Briles, D. E. (1991) · Microbial Pathogenesis · doi:10.1016/0882-4010(91)90033-7 · Cited by 21
Cited by
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Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
The Pleiotropic Two-Component Regulatory System PhoP-PhoQ
Groisman, E. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.6.1835-1842.2001 · Cited by 887
Self-citationAntimicrobial Peptides from Plants
Broekaert, W. F., Cammue, B. P. A., De Bolle, M. F. C., Thevissen, K., De Samblanx, G. W., Osborn, R. W., & Nielson, K. (1997) · Critical Reviews in Plant Sciences · doi:10.1080/07352689709701952 · Cited by 678
Lipid A Acylation and Bacterial Resistance against Vertebrate Antimicrobial Peptides
Guo, L., Lim, K. B., Poduje, C. M., Daniel, M., Gunn, J. S., Hackett, M., & Miller, S. I. (1998) · Cell · doi:10.1016/s0092-8674(00)81750-x · Cited by 649
Metadata
- Authors
- Groisman, E. A., Parra-Lopez, C., Salcedo, M., Lipps, C. J., & Heffron, F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-12-15
- Volume
- 89
- Issue
- 24
- Pages
- 11939-11943
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2041810355
- Cited by
- 265
- References
- 1
- FWCI
- 5.88
- Type
- journal article
- Language
- en
- Open access
- green
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- Groisman, E. A., Parra-Lopez, C., Salcedo, M., Lipps, C. J., & Heffron, F. (1992). Resistance to host antimicrobial peptides is necessary for Salmonella virulence. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.24.11939
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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