ArticleInfection and immunity2004
A novel lectin, DltA, is required for expression of a full serum resistance phenotype in 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 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Article
- Phosphoethanolamine Transferase LptA in Haemophilus ducreyi Modifies Lipid A and Contributes to Human Defensin Resistance In Vitro.PloS one · 2015Article
- Molecular phylogenetic analysis of non-sexually transmitted strains of Haemophilus ducreyi.PloS one · 2015Article
- Article
- Outer membrane protein P4 is not required for virulence in the human challenge model of Haemophilus ducreyi infection.BMC microbiology · 2014Article
- Trimeric autotransporter DsrA is a major mediator of fibrinogen binding in Haemophilus ducreyi.Infection and immunity · 2013Article
- Permeases of the sap transporter are required for cathelicidin resistance and virulence of Haemophilus ducreyi in humans.The Journal of infectious diseases · 2012Article
- Sialylation of lipooligosaccharides is dispensable for the virulence of Haemophilus ducreyi in humans.Infection and immunity · 2012Article
- An immunogenic, surface-exposed domain of Haemophilus ducreyi outer membrane protein HgbA is involved in hemoglobin binding.Infection and immunity · 2009Article
- Localization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin.Infection and immunity · 2009Article
- Outer membrane protein DsrA is the major fibronectin-binding determinant of Haemophilus ducreyi.Infection and immunity · 2008Article
- Dysregulated immune profiles for skin and dendritic cells are associated with increased host susceptibility to Haemophilus ducreyi infection in human volunteers.Infection and immunity · 2007Article
- Identification of genes involved in the expression of atypical lipooligosaccharide structures from a second class of Haemophilus ducreyi.Infection and immunity · 2007Article
- A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins.Journal of bacteriology · 2006Article
- A DltA mutant of Haemophilus ducreyi Is partially attenuated in its ability to cause pustules in human volunteers.Infection and immunity · 2006Article
- Identification of a novel sialic acid transporter in Haemophilus ducreyi.Infection and immunity · 2005Article
- Killing of dsrA mutants of Haemophilus ducreyi by normal human serum occurs via the classical complement pathway and is initiated by immunoglobulin M binding.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
5 authors at 4 institutions in 1 country.
Funding
Abstract
Haemophilus ducreyi, the causative agent of chancroid, is highly resistant to the complement-mediated bactericidal activity of normal human serum (NHS). Previously, we identified DsrA (for ducreyi serum resistance A), a major factor required for expression of the serum resistance phenotype in H. ducreyi. We describe here a second outer membrane protein, DltA (for ducreyi lectin A), which also contributes to serum resistance in H. ducreyi. Isogenic dltA mutants, constructed in 35000HP wild-type and FX517 dsrA backgrounds, were more susceptible to the bactericidal effects of NHS than each respective parent, demonstrating the additive effect of the mutations. Furthermore, expression of dltA in H. influenzae strain Rd rendered this highly susceptible strain partially resistant to 5% NHS compared to a vector-control strain. Although primary basic local alignment search tool analysis of the dltA open reading frame revealed no close bacterial homologue, similarity to the beta-chain of the eukaryotic lectin ricin was noted. DltA shares highly conserved structural motifs with the ricin beta chain, such as cysteines and lectin-binding domains. To determine whether dltA was a lectin, ligand blots and affinity chromatography experiments were performed. DltA was affinity purified on immobilized lactose and N-acetylgalactosamine, and N-glycosylated but not glycosidase-treated model glycoproteins bound DltA. These data indicate that DltA is a lectin with specificity for lactose-related carbohydrates (CHO) and is important for H. ducreyi serum resistance.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.