ArticleThe Journal of experimental medicine1999
Homologue scanning mutagenesis reveals CD66 receptor residues required for neisserial Opa protein binding.
Article in The Journal of experimental medicine, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- Imaging Flow Cytometry Analysis of CEACAM Binding to Opa-Expressing Neisseria gonorrhoeae.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2020Article
- Positive Selection Pressure Drives Variation on the Surface-Exposed Variable Proteins of the Pathogenic Neisseria.PloS one · 2016Article
- Mobile DNA in the pathogenicMicrobiology spectrum · 2015Article
- A comprehensive phylogenetic and structural analysis of the carcinoembryonic antigen (CEA) gene family.Genome biology and evolution · 2014Article
- Microbial antigenic variation mediated by homologous DNA recombination.FEMS microbiology reviews · 2012Review
- Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1.PloS one · 2011Article
- Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation.Molecular microbiology · 2008Article
- Opa proteins of pathogenic neisseriae initiate Src kinase-dependent or lipid raft-mediated uptake via distinct human carcinoembryonic antigen-related cell adhesion molecule isoforms.Infection and immunity · 2007Article
- Mutational analysis of human CEACAM1: the potential of receptor polymorphism in increasing host susceptibility to bacterial infection.Cellular microbiology · 2007Article
- A subfamily of Dr adhesins of Escherichia coli bind independently to decay-accelerating factor and the N-domain of carcinoembryonic antigen.The Journal of biological chemistry · 2006Article
- CEACAM engagement by human pathogens enhances cell adhesion and counteracts bacteria-induced detachment of epithelial cells.The Journal of cell biology · 2005Article
- Conservation of pregnancy-specific glycoprotein (PSG) N domains following independent expansions of the gene families in rodents and primates.BMC evolutionary biology · 2005Article
- Pathogenesis of Afa/Dr diffusely adhering Escherichia coli.Clinical microbiology reviews · 2005Review
- Article
- 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
- Specific regulation of T helper cell 1-mediated murine colitis by CEACAM1.The Journal of experimental medicine · 2004Article
- Carcinoembryonic antigen (CEA) and CEA-related cell adhesion molecule 1 (CEACAM1), apically expressed on human colonic M cells, are potential receptors for microbial adhesion.Histochemistry and cell biology · 2004Article
- Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in the CEA family.The EMBO journal · 2002Article
- Carcinoembryonic antigen family receptor recognition by gonococcal Opa proteins requires distinct combinations of hypervariable Opa protein domains.Infection and immunity · 2002Article
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
The immunoglobulin-like family of CD66 antigens, present on human neutrophils and epithelial cells, are used as receptors for adhesins expressed by the pathogenic Neisseriae. N. gonorrhoeae strain MS11 can express 11 isoforms of these adhesins, called opacity-related (Opa) proteins. Each MS11 Opa protein recognizes a distinct spectrum of CD66 receptors. CD66-Opa binding is mediated by the NH(2)-terminal domain of the receptor and occurs through protein-protein interactions. In this report, we have investigated the molecular basis for the binding between the CD66 and Opa protein families by mapping amino acids in CD66 receptors that determine Opa protein binding. We performed homologue scanning mutagenesis between CD66e, which binds multiple Opa variants, and CD66b, which binds none, and tested both loss-of-function by CD66e and gain-of-function by CD66b in solution assays and in assays involving full-length receptors expressed by epithelial cells. We found that three residues in the CD66e N-domain are required for maximal Opa protein receptor activity. Opa proteins that recognize the same spectrum of native CD66 molecules showed differential binding of receptors with submaximal activity, indicating that the binding characteristics of these Opa proteins are actually slightly different. These data provide a first step toward resolving the structural requirements for Opa-CD66 interaction.
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