ArticleJournal of bacteriology1997
The major outer membrane protein of Haemophilus ducreyi consists of two OmpA homologs.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 43 citations in OpenAlex.
- Role of OmpA1 and OmpA2 inJournal of oral microbiology · 2019Article
- Passive immunization with a polyclonal antiserum to the hemoglobin receptor of Haemophilus ducreyi confers protection against a homologous challenge in the experimental swine model of chancroid.Infection and immunity · 2011Article
- Characterization of the CpxRA regulon in Haemophilus ducreyi.Infection and immunity · 2010Article
- Characterization and comparative analysis of the genes encoding Haemophilus parasuis outer membrane proteins P2 and P5.Journal of bacteriology · 2009Article
- Comparative proteomic analysis of the Haemophilus ducreyi porin-deficient mutant 35000HP::P2AB.Journal of bacteriology · 2009Article
- Outer membrane protein DsrA is the major fibronectin-binding determinant of Haemophilus ducreyi.Infection and immunity · 2008Article
- A DltA mutant of Haemophilus ducreyi Is partially attenuated in its ability to cause pustules in human volunteers.Infection and immunity · 2006Article
- Haemophilus ducreyi Outer membrane determinants, including DsrA, define two clonal populations.Infection and immunity · 2005Article
- The UspA2 protein of Moraxella catarrhalis is directly involved in the expression of serum resistance.Infection and immunity · 2005Article
- Differential expression of porins OmpP2A and OmpP2B of Haemophilus ducreyi.Infection and immunity · 2004Article
- Sequence diversity and molecular evolution of the heat-modifiable outer membrane protein gene (ompA) of Mannheimia(Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi.Journal of bacteriology · 2004Article
- Expression of the LspA1 and LspA2 proteins by Haemophilus ducreyi is required for virulence in human volunteers.Infection and immunity · 2004Article
- The LspB protein is involved in the secretion of the LspA1 and LspA2 proteins by Haemophilus ducreyi.Infection and immunity · 2004Article
- Mutations in the lspA1 and lspA2 genes of Haemophilus ducreyi affect the virulence of this pathogen in an animal model system.Infection and immunity · 2003Article
- Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro.Infection and immunity · 2002Article
- Immunopathogenesis of Haemophilus ducreyi infection (chancroid).Infection and immunity · 2002Review
- Characterization of Haemophilus ducreyi cdtA, cdtB, and cdtC mutants in in vitro and in vivo systems.Infection and immunity · 2001Article
- Cloning, overexpression, purification, and immunobiology of an 85-kilodalton outer membrane protein from Haemophilus ducreyi.Infection and immunity · 2001Article
- Transcription of candidate virulence genes of Haemophilus ducreyi during infection of human volunteers.Infection and immunity · 2001Article
- Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and beta1,4-glucosyltransferase: identification of LOS glycoforms containing lactosamine repeats.Infection and immunity · 2000Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The major outer membrane protein (MOMP) of Haemophilus ducreyi is an OmpA homolog that migrates on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gels as three species with apparent molecular weights ranging from 37,000 to 43,000. Monoclonal antibodies directed against this macromolecule were used to identify recombinant clones containing fragments of the gene encoding this protein. Nucleotide sequence analysis of these fragments confirmed that the MOMP encoded by the intact gene (momp) was a member of the OmpA family of outer membrane proteins. Construction of an isogenic H. ducreyi mutant unable to express the MOMP led to the discovery of a second outer membrane protein which migrated at the same rate on SDS-PAGE gels as the MOMP. N-terminal amino acid sequence analysis of this second protein revealed that its N terminus was nearly identical to that of the MOMP and also had homology with members of the OmpA family. Nucleotide sequence analysis of the region downstream from the momp gene revealed the presence of a partial open reading frame encoding a predicted OmpA-like protein. A modification of anchored PCR technology was used to obtain the nucleotide sequence of this downstream gene which was shown to encode a second OmpA homolog (OmpA2). The N-terminal amino acid sequence of OmpA2 was identical to that of the OmpA-like protein detected in the momp mutant. The H. ducreyi MOMP and OmpA2 proteins, which comigrated on SDS-PAGE gels and which were encoded by the tandem arranged momp and ompA2 genes, were 72% identical.
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