ArticleProtein science : a publication of the Protein Society2006
Identification of surface-exposed components of MOMP of Chlamydia trachomatis serovar F.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 45 citations in OpenAlex.
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- Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection.Infection and immunity · 2022Article
- Overexpression of the Bam Complex Improves the Production ofInternational journal of molecular sciences · 2022Article
- A Chlamydia trachomatis VD1-MOMP vaccine elicits cross-neutralizing and protective antibodies against C/C-related complex serovars.NPJ vaccines · 2021Article
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- Ehrlichia chaffeensis EplA Interaction With Host Cell Protein Disulfide Isomerase Promotes Infection.Frontiers in cellular and infection microbiology · 2020Article
- Suppressors of Cytokine Signaling (SOCS)1 and SOCS3 Proteins Are Mediators of Interleukin-10 Modulation of Inflammatory Responses Induced byMediators of inflammation · 2020Article
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- Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation.Protein science : a publication of the Protein Society · 2018Article
- Engineering E. coli cell surface in order to develop a one-step purification method for recombinant proteins.AMB Express · 2018Article
- Novel Detection Strategy To Rapidly Evaluate the Efficacy of Antichlamydial Agents.Antimicrobial agents and chemotherapy · 2017Article
- Recombinant expression of Chlamydia trachomatis major outer membrane protein in E. Coli outer membrane as a substrate for vaccine research.BMC microbiology · 2016Article
- Anaplasma phagocytophilum Rab10-dependent parasitism of the trans-Golgi network is critical for completion of the infection cycle.Cellular microbiology · 2016Article
- Anaplasma phagocytophilum surface protein AipA mediates invasion of mammalian host cells.Cellular microbiology · 2014Article
- Increased immunoaccessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with Chlamydia muridarum.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Membrane vesicle production by Chlamydia trachomatis as an adaptive response.Frontiers in cellular and infection microbiology · 2014Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The identification of surface-exposed components of the major outer membrane protein (MOMP) of Chlamydia is critical for modeling its three-dimensional structure, as well as for understanding the role of MOMP in the pathogenesis of Chlamydia-related diseases. MOMP contains four variable domains (VDs). In this study, VDII and VDIV of Chlamydia trachomatis serovar F were proven to be surface-located by immuno-dot blot assay using monoclonal antibodies (MAbs). Two proteases, trypsin and endoproteinase Glu-C, were applied to digest the intact elementary body of serovar F under native conditions to reveal the surface-located amino acids. The resulting peptides were separated by SDS-PAGE and probed with MAbs against these VDs. N-terminal amino acid sequencing revealed: (1) The Glu-C cleavage sites were located within VDI (at Glu61) and VDIII (at Glu225); (2) the trypsin cleavage sites were found at Lys79 in VDI and at Lys224 in VDIII. The tryptic peptides were then isolated by HPLC and analyzed with a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer and a quadrupole-orthogonal-TOF mass spectrometer coupled with a capillary liquid chromatograph. Masses and fragmentation patterns that correlated to the peptides cleaved from VDI and VDIII regions, and C-terminal peptides Ser333-Arg358 and Ser333-Lys350 were observed. This result demonstrated that these regions are surface-exposed. Data derived from comparison of nonreduced outer membrane complex proteolytic fragments with their reduced fractions revealed that Cys26, 29, 33, 116, 208, and 337 were involved in disulfide bonds, and Cys26 and 337, and 116 and 208 were paired. Based on these data, a new two-dimensional model is proposed.
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