ArticleInfection and immunity2004
The LspB protein is involved in the secretion of the LspA1 and LspA2 proteins by Haemophilus ducreyi.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- Haemophilus ducreyi Seeks Alternative Carbon Sources and Adapts to Nutrient Stress and Anaerobiosis during Experimental Infection of Human Volunteers.Infection and immunity · 2016Article
- DksA and (p)ppGpp have unique and overlapping contributions to Haemophilus ducreyi pathogenesis in humans.Infection and immunity · 2015Article
- A (p)ppGpp-null mutant of Haemophilus ducreyi is partially attenuated in humans due to multiple conflicting phenotypes.Infection and immunity · 2014Article
- Article
- Haemophilus ducreyi Hfq contributes to virulence gene regulation as cells enter stationary phase.mBio · 2014Article
- The Haemophilus ducreyi Fis protein is involved in controlling expression of the lspB-lspA2 operon and other virulence factors.Infection and immunity · 2013Article
- System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.Journal of bacteriology · 2013Article
- Horizontal gene transfer in Histophilus somni and its role in the evolution of pathogenic strain 2336, as determined by comparative genomic analyses.BMC genomics · 2011Article
- A Haemophilus ducreyi CpxR deletion mutant is virulent in human volunteers.The Journal of infectious diseases · 2011Article
- Deletion of mtrC in Haemophilus ducreyi increases sensitivity to human antimicrobial peptides and activates the CpxRA regulon.Infection and immunity · 2011Article
- Characterization of the CpxRA regulon in Haemophilus ducreyi.Infection and immunity · 2010Article
- Activation of the CpxRA system by deletion of cpxA impairs the ability of Haemophilus ducreyi to infect humans.Infection and immunity · 2010Article
- Regulation of expression of the Haemophilus ducreyi LspB and LspA2 proteins by CpxR.Infection and immunity · 2009Article
- Two-partner secretion systems of Neisseria meningitidis associated with invasive clonal complexes.Infection and immunity · 2008Article
- Haemophilus ducreyi LspA proteins are tyrosine phosphorylated by macrophage-encoded protein tyrosine kinases.Infection and immunity · 2008Article
- Identification of gene products involved in biofilm production by Moraxella catarrhalis ETSU-9 in vitro.Infection and immunity · 2007Article
- Identification of a novel two-partner secretion locus in Moraxella catarrhalis.Infection and immunity · 2007Article
- Moraxella catarrhalis strain O35E expresses two filamentous hemagglutinin-like proteins that mediate adherence to human epithelial cells.Infection and immunity · 2007Article
- Haemophilus ducreyi targets Src family protein tyrosine kinases to inhibit phagocytic signaling.Infection and immunity · 2005Article
- Haemophilus ducreyi Outer membrane determinants, including DsrA, define two clonal populations.Infection and immunity · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The LspA1 and LspA2 proteins of Haemophilus ducreyi 35000 are two very large macromolecules that can be detected in concentrated culture supernatant fluid. Both of these proteins exhibit homology with the N-terminal region of the Bordetella pertussis filamentous hemagglutinin (FHA), which is involved in secretion of the latter macromolecule. The lspA2 open reading frame is flanked upstream by a gene, lspB, that encodes a predicted protein with homology to the B. pertussis FhaC outer membrane protein that is involved in secretion of FHA across the outer membrane. The H. ducreyi lspB gene encodes a protein with a predicted molecular mass of 66,573 Da. Reverse transcription-PCR analysis suggested that the lspB gene was transcribed together with the lspA2 gene on a single mRNA transcript. Polyclonal H. ducreyi LspB antiserum reacted with a 64-kDa antigen present in the Sarkosyl-insoluble cell envelope fraction of H. ducreyi 35000, which indicated that the LspB protein is likely an outer membrane protein. Concentrated culture supernatant fluids from H. ducreyi lspB and lspA1 lspB mutants did not contain detectable LspA1 and detectable LspA2, respectively. However, complementation of the lspB mutant with the wild-type lspB gene on a plasmid restored LspB protein expression and resulted in release of detectable amounts of the LspA1 protein into culture supernatant fluid. When evaluated in the temperature-dependent rabbit model of infection, the lspB mutant was attenuated in the ability to cause lesions and was never recovered in a viable form from lesions. These results indicated that the H. ducreyi LspB protein is involved in secretion of the LspA1 and LspA2 proteins across the outer membrane.
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