ArticleMolecular microbiology2010
Members of the Pmp protein family of Chlamydia pneumoniae mediate adhesion to human cells via short repetitive peptide motifs.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.
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Who cites it
58 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- Current status and future directions ofFrontiers in veterinary science · 2026Pooled it
- The distinct trimeric structure of the immunodominant chlamydial antigen Major Outer Membrane Protein.Nature communications · 2026Article
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- Pathogenicity and virulence ofVirulence · 2025Review
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- From coughs to complications: the story ofJournal of medical microbiology · 2025Review
- Genomic characteristics of emerging human pathogeniScience · 2025Article
- Immunization AgainstVaccines · 2025Article
- The secreted host-cell protein clusterin interacts with PmpD and promotesFrontiers in cellular and infection microbiology · 2024Article
- Sequence, structure prediction, and epitope analysis of the polymorphic membrane protein family in Chlamydia trachomatis.PloS one · 2024Article
- Genomic analysis of 61 Chlamydia psittaci strains reveals extensive divergence associated with host preference.BMC genomics · 2023Article
- Review
- Virulence Protein Pgp3 Is Insufficient To Mediate Plasmid-Dependent Infectivity of Chlamydia trachomatis.Infection and immunity · 2023Article
- Genome organization and genomics inFrontiers in cellular and infection microbiology · 2023Review
- Plasmid-mediated virulence inFrontiers in cellular and infection microbiology · 2023Review
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Article
- Prophylactic Multi-Subunit Vaccine againstVaccines · 2021Article
- Polymorphic Membrane Protein 17G ofFrontiers in immunology · 2021Article
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlamydiae sp. are obligate intracellular pathogens that cause a variety of diseases in humans. Adhesion of the infectious elementary body to the eukaryotic host cell is a pivotal step in chlamydial pathogenesis. Here we describe the characterization of members of the polymorphic membrane protein family (Pmp), the largest protein family (with up to 21 members) unique to Chlamydiaceae. We show that yeast cells displaying Pmp6, Pmp20 or Pmp21 on their surfaces, or beads coated with the recombinant proteins, adhere to human epithelial cells. A hallmark of the Pmp protein family is the presence of multiple repeats of the tetrapeptide motifs FxxN and GGA(I, L, V) and deletion analysis shows that at least two copies of these motifs are needed for adhesion. Importantly, pre-treatment of human cells with recombinant Pmp6, Pmp20 or Pmp21 protein reduces infectivity upon subsequent challenge with Chlamydia pneumoniae and correlates with diminished attachment of Chlamydiae to target cells. Antibodies specific for Pmp21 can neutralize infection in vitro. Finally, a combination of two different Pmp proteins in infection blockage experiments shows additive effects, possibly suggesting similar functions. Our findings imply that Pmp6, Pmp20 and Pmp21 act as adhesins, are vital during infection and thus represent promising vaccine candidates.
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