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A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectin
MB Brinkman, MA McGill, J Pettersson, A Rogers, P Matejkova, D Smajs, GM Weinstock, SJ Norris, T Palzkill
Jazyk angličtina Země Spojené státy americké
Typ dokumentu Research Support, N.I.H., Extramural, práce podpořená grantem
NLK
Free Medical Journals
od 1970 do Před 6 měsíci
Freely Accessible Science Journals
od 1995 do Před 6 měsíci
PubMed Central
od 1970 do Před 1 rokem
Europe PubMed Central
od 1970 do Před 6 měsíci
Open Access Digital Library
od 1970-01-01
Open Access Digital Library
od 1970-01-01
PubMed
18332212
DOI
10.1128/iai.01424-07
Knihovny.cz E-zdroje
- MeSH
- bakteriální vakcíny MeSH
- DNA bakterií genetika chemie MeSH
- fibronektiny * metabolismus MeSH
- fluorescenční mikroskopie MeSH
- imunoelektronová mikroskopie MeSH
- králíci MeSH
- laminin * metabolismus MeSH
- lidé MeSH
- molekulární sekvence - údaje MeSH
- polymorfismus genetický MeSH
- proteiny vnější bakteriální membrány genetika imunologie izolace a purifikace metabolismus MeSH
- protilátky bakteriální genetika imunologie izolace a purifikace krev metabolismus MeSH
- rekombinantní proteiny imunologie MeSH
- Treponema pallidum * MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
The antigenicity, structural location, and function of the predicted lipoprotein TP0136 of Treponema pallidum subsp. pallidum were investigated based on previous screening studies indicating that anti-TP0136 antibodies are present in the sera of syphilis patients and experimentally infected rabbits. Recombinant TP0136 (rTP0136) protein was purified and shown to be strongly antigenic during human and experimental rabbit infection. The TP0136 protein was exposed on the surface of the bacterial outer membrane and bound to the host extracellular matrix glycoproteins fibronectin and laminin. In addition, the TP0136 open reading frame was shown to be highly polymorphic among T. pallidum subspecies and strains at the nucleotide and amino acid levels. Finally, the ability of rTP0136 protein to act as a protective antigen to subsequent challenge with infectious T. pallidum in the rabbit model of infection was assessed. Immunization with rTP0136 delayed ulceration but did not prevent infection or the formation of lesions. These results demonstrate that TP0136 is expressed on the outer membrane of the treponeme during infection and may be involved in attachment to host extracellular matrix components.
Citace poskytuje Crossref.org
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- $a The antigenicity, structural location, and function of the predicted lipoprotein TP0136 of Treponema pallidum subsp. pallidum were investigated based on previous screening studies indicating that anti-TP0136 antibodies are present in the sera of syphilis patients and experimentally infected rabbits. Recombinant TP0136 (rTP0136) protein was purified and shown to be strongly antigenic during human and experimental rabbit infection. The TP0136 protein was exposed on the surface of the bacterial outer membrane and bound to the host extracellular matrix glycoproteins fibronectin and laminin. In addition, the TP0136 open reading frame was shown to be highly polymorphic among T. pallidum subspecies and strains at the nucleotide and amino acid levels. Finally, the ability of rTP0136 protein to act as a protective antigen to subsequent challenge with infectious T. pallidum in the rabbit model of infection was assessed. Immunization with rTP0136 delayed ulceration but did not prevent infection or the formation of lesions. These results demonstrate that TP0136 is expressed on the outer membrane of the treponeme during infection and may be involved in attachment to host extracellular matrix components.
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