ArticleBMC genomics2011
Multi-genome identification and characterization of chlamydiae-specific type III secretion substrates: the Inc proteins.
Article in BMC genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 135 citations in OpenAlex.
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
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- The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection.Cell reports · 2025Article
- Inc/GFP chimera protein-based interactomics reveals host cellular interactions of Cps0558, a novel Chlamydia psittaci inclusion protein.Pathogens and disease · 2025Article
- The T3SS structural and effector genes ofFrontiers in cellular and infection microbiology · 2025Article
- The acetylase activity of Cdu1 regulates bacterial exit from infected cells by protectingeLife · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Whole Genome Sequencing and Comparative Genomic Analysis ofPathogens (Basel, Switzerland) · 2023Article
- Article
- A Functional Yeast-Based Screen Identifies the Host Microtubule Cytoskeleton as a Target of NumerousInternational journal of molecular sciences · 2023Article
- The Chlamydia trachomatis IncM Protein Interferes with Host Cell Cytokinesis, Centrosome Positioning, and Golgi Distribution and Contributes to the Stability of the Pathogen-Containing Vacuole.Infection and immunity · 2023Article
- Molecular pathogenesis ofFrontiers in cellular and infection microbiology · 2023Review
- Review
- Genome organization and genomics inFrontiers in cellular and infection microbiology · 2023Review
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- The bacterial effector GarD shields Chlamydia trachomatis inclusions from RNF213-mediated ubiquitylation and destruction.Cell host & microbe · 2022Article
- The inclusion membrane protein IncS is critical for initiation of the Chlamydia intracellular developmental cycle.PLoS pathogens · 2022Article
- Article
- TheInfection and immunity · 2022Article
- The Chlamydia trachomatis inclusion membrane protein CT006 associates with lipid droplets in eukaryotic cells.PloS one · 2022Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundChlamydiae are obligate intracellular bacteria that multiply in a vacuolar compartment, the inclusion. Several chlamydial proteins containing a bilobal hydrophobic domain are translocated by a type III secretion (TTS) mechanism into the inclusion membrane. They form the family of Inc proteins, which is specific to this phylum. Based on their localization, Inc proteins likely play important roles in the interactions between the microbe and the host. In this paper we sought to identify and analyze, using bioinformatics tools, all putative Inc proteins in published chlamydial genomes, including an environmental species.
resultsInc proteins contain at least one bilobal hydrophobic domain made of two transmembrane helices separated by a loop of less than 30 amino acids. Using bioinformatics tools we identified 537 putative Inc proteins across seven chlamydial proteomes. The amino-terminal segment of the putative Inc proteins was recognized as a functional TTS signal in 90% of the C. trachomatis and C. pneumoniae sequences tested, validating the data obtained in silico. We identified a macro domain in several putative Inc proteins, and observed that Inc proteins are enriched in segments predicted to form coiled coils. A surprisingly large proportion of the putative Inc proteins are not constitutively translocated to the inclusion membrane in culture conditions.
conclusionsThe Inc proteins represent 7 to 10% of each proteome and show a great degree of sequence diversity between species. The abundance of segments with a high probability for coiled coil conformation in Inc proteins support the hypothesis that they interact with host proteins. While the large majority of Inc proteins possess a functional TTS signal, less than half may be constitutively translocated to the inclusion surface in some species. This suggests the novel finding that translocation of Inc proteins may be regulated by as-yet undetermined mechanisms.
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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.