{"doi":"10.3201/eid0301.970102","title":"Surface Antigens of the Syphilis Spirochete and Their Potential as Virulence Determinants","abstract":null,"journal":"Emerging Infectious Diseases","year":1997,"id":657581,"datarank":2.640928462046744,"base_score":3.784189633918261,"endowment":3.784189633918261,"self_citation_contribution":0.5676284450877392,"citation_network_contribution":2.073300016959005,"self_endowment_contribution":0.5676284450877392,"citer_contribution":2.073300016959005,"corpus_percentile":null,"corpus_rank":null,"citation_count":43,"citer_count":42,"citers_with_citation_signal":37,"citers_with_endowment":37,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Surface Antigens of the Syphilis Spirochete and Their Potential as Virulence Determinants","abstract":"A unique physical feature of Treponema pallidum, the venereally transmitted agent of human syphilis, is that its outer membrane contains 100-fold less membrane-spanning protein than the outer membranes of typical gram-negative bacteria, a property that has been related to the chronicity of syphilitic infection. These membrane-spanning T. pallidum rare outer membrane proteins, termed TROMPs, represent potential surface-exposed virulence determinants and targets of host immunity. Only recently has the outer membrane of T. pallidum been isolated and its constituent proteins identified. Five proteins of molecular mass 17-, 28-, 31-, 45-, and 65-kDa were outer membrane associated. The 17- and 45-kDa proteins, which are also present in greater amounts with the T. pallidum inner membrane protoplasmic cylinder complex, had been previously characterized lipoproteins and are, therefore, not membrane-spanning but rather membrane-anchored by their lipid moiety. In contrast, the 28-, 31-, and 65-kDa proteins are exclusively associated with the outer membrane. Both the purified native and an Escherichia coli recombinant outer membrane form of the 31-kDa protein, designated Tromp1, exhibit porin activity, thereby confirming the membrane-spanning outer membrane topology of Tromp1. The 28-kDa protein, designated Tromp2, has sequence characteristics in common with membrane-spanning outer membrane proteins and has also been recombinantly expressed in E. coli, where it targets exclusively to the E. coli outer membrane. The 65-kDa protein, designated Tromp3, is present in the least amount relative to Tromps1 and 2. Tromps 1, 2, and 3 were antigenic when tested with serum from infection and immune syphilitic rabbits and humans. These newly identified TROMPs provide a molecular foundation for the future study of syphilis pathogenesis and immunity.","is_dataset_classified":null,"base_score":3.784189633918261,"endowment":3.784189633918261,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9126440","pmcid":"PMC2627599","openalex_id":"https://openalex.org/W2146899109","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"3U50CK000379-01S1","title":"The Affordable Care Act: Building Epidemiology, Laboratory, and Health Information Systems Capacity"}],"total_grants":1,"fwci":0.9427,"citation_percentile":0.74826533,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2014,"count":3},{"year":2015,"count":2},{"year":2016,"count":1},{"year":2017,"count":4},{"year":2019,"count":2},{"year":2020,"count":1},{"year":2022,"count":2},{"year":2023,"count":1},{"year":2024,"count":2},{"year":2026,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.3201/eid0301.970102","host_type":"journal"},{"url":"https://doi.org/10.3201/eid0301.970102","host_type":"publisher"},{"url":"https://wwwnc.cdc.gov/eid/article/3/1/97-0102_article","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9126440","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC2627599","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2627599","host_type":"repository"},{"url":"https://doaj.org/article/be503d61a6bb4d9eb2ecb0730667190e","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC2627599","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC2627599?pdf=render","host_type":"Europe_PMC"},{"url":"https://wwwnc.cdc.gov/eid/content/24/10/pdfs/v24-n10.pdf","host_type":""},{"url":"https://dx.doi.org/10.3201/eid0301.970102","host_type":""}],"fields_of_study":["Syphilis Diagnosis and Treatment","Reproductive tract infections research","Antimicrobial Peptides and Activities","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Antigens, Bacterial","Antigens, Surface","Bacterial Outer Membrane Proteins","Bacterial Proteins","Escherichia coli","Freeze Fracturing","Humans","Membrane Proteins","Microscopy, Electron","Porins","Rabbits","Recombinant Proteins","Syphilis","Treponema pallidum","Virulence"],"mesh_terms":["Animals","Antigens, Bacterial","Antigens, Surface","Bacterial Outer Membrane Proteins","Bacterial Proteins","Escherichia coli","Freeze Fracturing","Humans","Membrane Proteins","Microscopy, Electron","Rabbits","Recombinant Proteins","Syphilis","Treponema pallidum","Virulence","Porins"],"keywords":["Bacterial outer membrane","Porin","Treponema","Membrane protein","Outer membrane efflux proteins","Biology","Inner membrane","Periplasmic space","Peripheral membrane protein","Vesicle-associated membrane protein 8","Virulence","Integral membrane protein","Escherichia coli","Microbiology","Membrane","Biochemistry","Virology","Syphilis","Gene","Antigens, Bacterial","R","Membrane Proteins","Porins","Infectious and parasitic diseases","RC109-216","United States","Recombinant Proteins","Microscopy, Electron","Bacterial Proteins","Antigens, Surface","Medicine","Animals","Freeze Fracturing","Humans","Rabbits","Treponema pallidum","Bacterial Outer Membrane Proteins"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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