ArticleJournal of bacteriology1998
Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 51 citations in OpenAlex.
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Stealthy microbes: HowFrontiers in cellular and infection microbiology · 2022Review
- Neisseria gonorrhoeae host adaptation and pathogenesis.Nature reviews. Microbiology · 2018Review
- Lactoferrin binding protein B - a bi-functional bacterial receptor protein.PLoS pathogens · 2017Article
- Metal limitation and toxicity at the interface between host and pathogen.FEMS microbiology reviews · 2014Review
- The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides.PloS one · 2014Article
- NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface.Infection and immunity · 2010Article
- Iron transport systems in Neisseria meningitidis.Microbiology and molecular biology reviews : MMBR · 2004Review
- Gonococcal genes encoding transferrin-binding proteins A and B are arranged in a bicistronic operon but are subject to differential expression.Infection and immunity · 2001Article
- Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus.Journal of bacteriology · 2000Article
- Antigenic and sequence diversity in gonococcal transferrin-binding protein A.Infection and immunity · 2000Article
- Identification of a human lactoferrin-binding protein in Gardnerella vaginalis.Infection and immunity · 2000Article
- Isolation of Neisseria gonorrhoeae mutants that show enhanced trafficking across polarized T84 epithelial monolayers.Infection and immunity · 2000Article
- Analysis of the immunological responses to transferrin and lactoferrin receptor proteins from Moraxella catarrhalis.Infection and immunity · 1999Article
- Characterization of Moraxella (Branhamella) catarrhalis lbpB, lbpA, and lactoferrin receptor orf3 isogenic mutants.Infection and immunity · 1999Article
- Identification and functional characterization of the Neisseria gonorrhoeae lbpB gene product.Infection and immunity · 1999Article
Corrections and comments
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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
Pathogenic members of the family Neisseriaceae produce specific receptors facilitating iron acquisition from transferrin (Tf) and lactoferrin (Lf) of their mammalian host. Tf receptors are composed of two outer membrane proteins, Tf-binding proteins A and B (TbpA and TbpB; formerly designated Tbp1 and Tbp2, respectively). Although only a single Lf-binding protein, LbpA (formerly designated Lbp1), had previously been recognized, we recently identified additional bacterial Lf-binding proteins in the human pathogens Neisseria meningitidis and Moraxella catarrhalis and the bovine pathogen Moraxella bovis by a modified affinity isolation technique (R. A. Bonnah, R.-H. Yu, and A. B. Schryvers, Microb. Pathog. 19:285-297, 1995). In this report, we characterize an open reading frame (ORF) located immediately upstream of the N. meningitidis B16B6 lbpA gene. Amino acid sequence comparisons of various TbpBs with the product of the translated DNA sequence from the upstream ORF suggests that the region encodes the Lf-binding protein B homolog (LbpB). The LbpB from strain B16B6 has two large stretches of negatively charged amino acids that are not present in the various transferrin receptor homologs (TbpBs). Expression of the recombinant LbpB protein as a fusion with maltose binding protein demonstrated functional Lf-binding activity. Studies with N. meningitidis isogenic mutants in which the lbpA gene and the ORF immediately upstream of lbpA (putative lbpB gene) were insertionally inactivated demonstrated that LbpA, but not LbpB, is essential for iron acquisition from Lf in vitro.
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