ArticleInfection and immunity1994
Heat shock response and heat shock protein antigens of Vibrio cholerae.
Article in Infection and immunity, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Silencing of heat shock protein 90 (hsp90): Effect on development and infectivity of Ichthyophthirius multifiliis.BMC veterinary research · 2023Article
- Sequence Determinants Spanning -10 Motif and Spacer Region Implicated in UniqueFrontiers in microbiology · 2019Article
- Cloning, expression, purification, crystallization and preliminary X-ray analysis of the 31 kDa Vibrio cholerae heat-shock protein VcHsp31.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Enterotoxigenic Escherichia coli elicits immune responses to multiple surface proteins.Infection and immunity · 2010Article
- Global gene expression and phenotypic analysis of a Vibrio cholerae rpoH deletion mutant.Journal of bacteriology · 2007Article
- Identification of DnaJ-like chaperone in Clostridium botulinum type A.Journal of protein chemistry · 1999Article
- Role of DnaK in in vitro and in vivo expression of virulence factors of Vibrio cholerae.Infection and immunity · 1999Article
- Porins of Vibrio cholerae: purification and characterization of OmpU.Journal of bacteriology · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sixteen heat shock proteins (Hsps) have been identified in the hypertoxinogenic strain 569B of Vibrio cholerae which are synthesized in response to small and large elevations of temperature. The induction of the Hsps is necessary for the cells to survive the deleterious effects of heat. There is no difference in the pattern of induction of the Hsps in V. cholerae strains varying in levels of toxinogenicity. One of the major low-molecular-mass Hsps, a 16-kDa protein, is preferentially degraded following shift down of temperature. This protein is induced at a much lower level at high temperatures in cells maintained in the laboratory for a prolonged period. The only Hsp located in the outer membrane of V. cholerae cells is a 23-kDa protein. Western immunoblot analysis with human immune sera collected from convalescent cholera patients revealed that this protein is markedly immunogenic. The human immune serum also reacted with the 69- and 16-kDa major Hsps and the 88-, 66-, and 46-kDa Hsps but not with the 61-kDa major Hsp identified as the groEL gene product. All major Hsps reacted with rabbit anti-V. cholerae sera. Ethanol stress leads to the induction of four of the major Hsps and three additional proteins.
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Registered trials
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