ArticleInfection and immunity1992
A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus.
Article in Infection and immunity, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 162 citations in OpenAlex.
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- Proteomic approach to identify host cell attachment proteins provides protective Pseudomonas aeruginosa vaccine antigen FtsZ.NPJ vaccines · 2024Article
- Molecular Identification and Bioinformatics Analysis ofPathogens (Basel, Switzerland) · 2024Article
- Moonlighting genes harbor antisense ORFs that encode potential membrane proteins.Scientific reports · 2023Article
- Priestia flexa KS1: A new bacterial strain isolated from human faeces implicated in mucin degradation.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Sharing of Moonlighting Proteins Mediates the Symbiotic Relationship among Intestinal Commensals.Applied and environmental microbiology · 2023Article
- Silencing of heat shock protein 90 (hsp90): Effect on development and infectivity of Ichthyophthirius multifiliis.BMC veterinary research · 2023Article
- Heating Rate during Shell Egg Thermal Treatment Elicits Stress Responses and Alters Virulence of Salmonella enterica Serovar Enteritidis; Implications for Shell Egg Pasteurization.Applied and environmental microbiology · 2022Article
- Moonlighting in Rickettsiales: Expanding Virulence Landscape.Tropical medicine and infectious disease · 2022Review
- Proteins of the Ciliated Protozoan ParasitePathogens (Basel, Switzerland) · 2021Article
- GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages.BMC microbiology · 2021Article
- Article
- Secretion Systems in Gram-Negative Bacterial Fish Pathogens.Frontiers in microbiology · 2021Review
- Understanding GroEL and DnaK Stress Response Proteins as Antigens for Bacterial Diseases.Vaccines · 2020Review
- Galectin-2 Has Bactericidal Effects againstInternational journal of molecular sciences · 2020Article
- Subcellular Location ofMicroorganisms · 2020Article
- Non-surface Attached Bacterial Aggregates: A Ubiquitous Third Lifestyle.Frontiers in microbiology · 2020Review
- GroEL Protein (Heat Shock Protein 60) of Mycoplasma gallisepticum Induces Apoptosis in Host Cells by Interacting with Annexin A2.Infection and immunity · 2019Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salmonella typhimurium infections have increased during the last few years. However, the interplay of virulence factors in S. typhimurium pathogenesis is still poorly understood, particularly with regard to the mechanisms and components of the bacterium which are involved in its interaction with the intestinal mucus. We have observed that S. typhimurium is aggregated by incubation with colonic mucus (guinea pig model). To quantify this phenomenon, an aggregation assay was established. By using this assay, it was found that the aggregation profile of S. typhimurium strains freshly isolated from patients (age 9 and older) with salmonellosis correlated with the severity of the disease. An isolate with high aggregation behavior was chosen for characterization of the bacterial component involved in binding to colonic mucus material. The component of S. typhimurium responsible for aggregation was purified and characterized as a 66-kDa protein which was able to completely inhibit mucus-mediated bacterial aggregation. This protein was recognized by monoclonal antibodies against the 65-kDa heat shock protein (HSP) of Mycobacterium leprae. The 66-kDa protein of S. typhimurium was inducible by incubating the bacteria at 50 degrees C and was secreted into the supernatant, from which it could be isolated in both dimeric and polymeric forms. The monoclonal anti-HSP 65, as well as a polyclonal antibody against the 66-kDa protein of S. typhimurium, caused dose-dependent inhibition of the aggregation of S. typhimurium by crude mucus preparations. This is the first report showing that a bacterial HSP is involved in mucus-mediated interaction of pathogens with the host.
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