ArticleInfection and immunity1998
The major outer membrane protein of Chlamydia psittaci functions as a porin-like ion channel.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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
25 citing papers in PubMed, 68 citations in OpenAlex.
- The distinct trimeric structure of the immunodominant chlamydial antigen Major Outer Membrane Protein.Nature communications · 2026Article
- Article
- Identification of proteins differentially expressed by Chlamydia trachomatis treated with chlamydiaphage capsid protein VP1 during intracellular growth.Archives of microbiology · 2017Article
- Pathogenic outcome following experimental infection of sheep with Chlamydia abortus variant strains LLG and POS.PloS one · 2017Article
- Intramuscular Immunisation with Chlamydial Proteins Induces Chlamydia trachomatis Specific Ocular Antibodies.PloS one · 2015Article
- Benzylidene acylhydrazides inhibit chlamydial growth in a type III secretion- and iron chelation-independent manner.Journal of bacteriology · 2014Article
- Article
- Detection and identification of Chlamydophila psittaci in asymptomatic parrots in Poland.BMC veterinary research · 2012Article
- Identification of immunologically relevant proteins of Chlamydophila abortus using sera from experimentally infected pregnant ewes.Clinical and vaccine immunology : CVI · 2010Article
- Comprehensive in silico prediction and analysis of chlamydial outer membrane proteins reflects evolution and life style of the Chlamydiae.BMC genomics · 2009Article
- The outer membrane protein VhOmp of Vibrio harveyi: pore-forming properties in black lipid membranes.The Journal of membrane biology · 2009Article
- Porin activity of Anaplasma phagocytophilum outer membrane fraction and purified P44.Journal of bacteriology · 2007Article
- Identification of surface-exposed components of MOMP of Chlamydia trachomatis serovar F.Protein science : a publication of the Protein Society · 2006Article
- Surface expression, single-channel analysis and membrane topology of recombinant Chlamydia trachomatis Major Outer Membrane Protein.BMC microbiology · 2005Article
- Expression and refolding of Omp38 from Burkholderia pseudomallei and Burkholderia thailandensis, and its function as a diffusion porin.The Biochemical journal · 2004Article
- Diagnosis and assessment of trachoma.Clinical microbiology reviews · 2004Review
- Production of Chlamydia pneumoniae proteins in Bacillus subtilis and their use in characterizing immune responses in the experimental infection model.Clinical and diagnostic laboratory immunology · 2003Article
- Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia.Protein science : a publication of the Protein Society · 2002Article
- Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds.Infection and immunity · 2002Article
- Chlamydial infection in sheep: immune control versus fetal pathology.Journal of the Royal Society of Medicine · 2001Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major outer membrane protein (MOMP) of Chlamydia species shares several biochemical properties with classical porin proteins. Secondary structure analysis by circular dichroism now reveals that MOMP purified from Chlamydia psittaci has a predominantly beta-sheet content (62%), which is also typical of bacterial porins. Can MOMP form functional ion channels? To directly test the "porin channel" hypothesis at the molecular level, the MOMP was reconstituted into planar lipid bilayers, where it gave rise to multibarreled channels, probably trimers, which were modified by an anti-MOMP monoclonal antibody. These observations are consistent with the well-characterized homo-oligomeric nature of MOMP previously revealed by biochemical analysis and with the triple-barreled behavior of other porins. MOMP channels were weakly anion selective (PCl/PK approximately 2) and permeable to ATP. They may therefore be a route by which Chlamydia can take advantage of host nucleoside triphosphates and explain why some anti-MOMP antibodies neutralize infection. These findings have broad implications on the search for an effective chlamydial vaccine to control the significant human and animal diseases caused by these organisms.
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