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Titolo:
Post-translational modification of the myxoma-virus anti-inflammatory serpin SERP-1 by a virally encoded sialyltransferase
Autore:
Nash, P; Barry, M; Seet, BT; Veugelers, K; Hota, S; Heger, J; Hodgkinson, G; Graham, K; Jackson, RJ; McFadden, G;
Indirizzi:
Univ Western Ontario, John P Robarts Res Inst, London, ON N6G 2V4, Canada Univ Western Ontario London ON Canada N6G 2V4 London, ON N6G 2V4, Canada Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada Univ Alberta Edmonton AB Canada T6G 2H7 hem, Edmonton, AB T6G 2H7, Canada Univ Western Ontario, Dept Microbiol & Immunol, London, ON N6G 2V4, CanadaUniv Western Ontario London ON Canada N6G 2V4 London, ON N6G 2V4, Canada CSIRO Wildlife & Ecol, CRC, Pest Anim Control, Canberra, ACT 2601, Australia CSIRO Wildlife & Ecol Canberra ACT Australia 2601 ra, ACT 2601, Australia
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 347, anno: 2000,
parte:, 2
pagine: 375 - 382
SICI:
0264-6021(20000415)347:<375:PMOTMA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE PROTEINASE-INHIBITOR; RABBIT FIBROMA VIRUS; QUALITY-CONTROL; ENDOPLASMIC-RETICULUM; PLASMINOGEN-ACTIVATOR; SECRETORY PATHWAY; SIALIC ACIDS; GLYCOPROTEINS; MECHANISM; SURFACE;
Keywords:
glycosylation; poxvirus; proteinase; sialylation; virulence factor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: McFadden, G Univ Western Ontario, John P Robarts Res Inst, London, ON N6G 2V4, Canada Univ Western Ontario London ON Canada N6G 2V4 N6G 2V4, Canada
Citazione:
P. Nash et al., "Post-translational modification of the myxoma-virus anti-inflammatory serpin SERP-1 by a virally encoded sialyltransferase", BIOCHEM J, 347, 2000, pp. 375-382

Abstract

SERP-1 is a secreted serpin (serine-proteinase inhibitor) encoded by myxoma virus, a poxvirus pathogen of rabbits. SERP-1 is required for myxoma-virus virulence, and the purified protein has been shown to possess independentanti-inflammatory activity in animal models of restenosis and antigen-induced arthritis. As an inhibitor of serine proteinases, SERP-1 acts against tissue-type plasminogen activator, urokinase-type plasminogen activator, plasmin, thrombin and Factor Xa. In the present study, examination of SERP-1 glycosylation-site mutants showed that the N-linked glycosylation of Asn(172) was essential for SERP-1 secretion, whereas mutation of Asn(99) decreasedsecretion efficiency, indicating that N-linked glycosylation plays an essential role in the processing and trafficking of SERP-1. Furthermore, comparison of SERP-1 from wild-type myxoma virus and a virus containing a targeted disruption of the MST3N sialyltransferase locus demonstrated that SERP-1 is specifically modified by this myxoma-virus-encoded sialyltransferase, and is thus the first reported viral protein shown to by modified by a virally encoded glycosyltransferase. Sialylation of SERP-1 by the MST3N gene product creates a uniquely charged species of secreted SERP-1 that is distinct from SERP-1 produced From other eukaryotic expression systems, though this has no apparent effect upon the kinetics of in vitro proteinase inhibition. Rather, the role of viral sialylation of SERP-1 likely relates to masking antigenicity or targeting SERP-1 to specific sites of action in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:30:34