ArticleThe Journal of biological chemistry2011
Neisseria meningitidis adhesin NadA targets beta1 integrins: functional similarity to Yersinia invasin.
Article in The Journal of biological chemistry, 2011. 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, 50 citations in OpenAlex.
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- Product review on the IMD serogroup B vaccine Bexsero®.Human vaccines & immunotherapeutics · 2022Article
- Structural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin.Cell reports · 2022Article
- The Host-Pathogen Interactions and Epicellular Lifestyle ofFrontiers in cellular and infection microbiology · 2022Review
- Capsule-dependent impact of MAPK signalling on host cell invasion and immune response during infection of the choroid plexus epithelium by Neisseria meningitidis.Fluids and barriers of the CNS · 2021Article
- Article
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Immunogenicity of trimeric autotransporter adhesins and their potential as vaccine targets.Medical microbiology and immunology · 2020Review
- A simple and rapid pipeline for identification of receptor-binding sites on the surface proteins of pathogens.Scientific reports · 2020Article
- Virulence Factors of Meningitis-Causing Bacteria: Enabling Brain Entry across the Blood-Brain Barrier.International journal of molecular sciences · 2019Review
- The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease.Pathogens and disease · 2017Review
- A journey into the brain: insight into how bacterial pathogens cross blood-brain barriers.Nature reviews. Microbiology · 2017Review
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- An international invasive meningococcal disease outbreak due to a novel and rapidly expanding serogroup W strain, Scotland and Sweden, July to August 2015.Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2016Article
- Exploring host-pathogen interactions through genome wide protein microarray analysis.Scientific reports · 2016Article
- Neisseria cinerea isolates can adhere to human epithelial cells by type IV pilus-independent mechanisms.Microbiology (Reading, England) · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Meningococci are facultative-pathogenic bacteria endowed with a set of adhesins allowing colonization of the human upper respiratory tract, leading to fulminant meningitis and septicemia. The Neisseria adhesin NadA was identified in about 50% of N. meningitidis isolates and is closely related to the Yersinia adhesin YadA, the prototype of the oligomeric coiled-coil adhesin (Oca) family. NadA is known to be involved in cell adhesion, invasion, and induction of proinflammatory cytokines. Because of the enormous diversity of neisserial cell adhesins the analysis of the specific contribution of NadA in meningococcal host interactions is limited. Therefore, we used a non-invasive Y. enterocolitica mutant as carrier to study the role of NadA in host cell interaction. NadA was shown to be efficiently produced and localized in its oligomeric form on the bacterial surface of Y. enterocolitica. Additionally, NadA mediated a β1 integrin-dependent adherence with subsequent internalization of yersiniae by a β1 integrin-positive cell line. Using recombinant NadA(24-210) protein and human and murine β1 integrin-expressing cell lines we could demonstrate the role of the β1 integrin subunit as putative receptor for NadA. Subsequent inhibition assays revealed specific interaction of NadA(24-210) with the human β1 integrin subunit. Cumulatively, these results indicate that Y. enterocolitica is a suitable toolbox system for analysis of the adhesive properties of NadA, revealing strong evidence that β1 integrins are important receptors for NadA. Thus, this study demonstrated for the first time a direct interaction between the Oca-family member NadA and human β1 integrins.
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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.