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Titolo:
THE NEMATOPHAGOUS FUNGUS VERTICILLIUM-CHLAMYDOSPORIUM PRODUCES A CHYMOELASTASE-LIKE PROTEASE WHICH HYDROLYZES HOST NEMATODE PROTEINS IN-SITU
Autore:
SEGERS R; BUTT TM; KERRY BR; PEBERDY JF;
Indirizzi:
ROTHAMSTED EXPTL STN,DEPT ENTOMOL & NEMATOL HARPENDEN AL5 2JQ HERTS ENGLAND UNIV NOTTINGHAM,DEPT LIFE SCI NOTTINGHAM NG7 2RD ENGLAND
Titolo Testata:
Microbiology
, volume: 140, anno: 1994,
parte:, 10
pagine: 2715 - 2723
SICI:
1350-0872(1994)140:<2715:TNFVPA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CEREAL CYST-NEMATODE; EXTRACELLULAR PROTEASES; METARHIZIUM-ANISOPLIAE; HETERODERA-AVENAE; PARASITISM; SUBSTRATE; EGGS; SUCHLASPORIUM; PURIFICATION; VIRULENCE;
Keywords:
CHYMOTRYPSIN; CHYMOELASTASE; PROTEASE; NEMATOPHAGOUS FUNGUS; VERTICILLIUM CHLAMYDOSPORIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
R. Segers et al., "THE NEMATOPHAGOUS FUNGUS VERTICILLIUM-CHLAMYDOSPORIUM PRODUCES A CHYMOELASTASE-LIKE PROTEASE WHICH HYDROLYZES HOST NEMATODE PROTEINS IN-SITU", Microbiology, 140, 1994, pp. 2715-2723

Abstract

The nematophagous fungus Verticillium chlamydosporium secreted several proteases in submerged culture in which soya peptone was the sole carbon and nitrogen source. One protease, VCP1 (M(r) 33000, pI 10.2), was purified 14-fold from culture filtrates to apparent homogeneity using preparative isoelectric focusing in free solution, and shown to rapidly hydrolyse the chymotrypsin substrate Suc-(Ala)(2)-Pro-Phe-pNA and elastin. VCP1 had a K-m for Suc-(Ala)(2)-Pro-Phe-pNA of 4.3 x 10(-5) Mand a k(cat) of 5.8 s(-1). It was highly sensitive to PMSF and TPCK, but only moderately sensitive to chicken egg-white and soya bean trypsin inhibitors. VCP1 degraded a wide range of polymeric substrates, including Azocoll, hide protein, elastin, casein and albumin, and accounted for most of the non-specific protease activity detected in culture filtrates. The purified enzyme hydrolysed proteins in situ from the outer layer of the egg shell of the host nematode Meloidogyne incognita and exposed its chitin layer. VCP1 was secreted by several isolates ofV. chlamydosporium and V. lecanii, pathogens of nematodes and insectsrespectively, but not plant-pathogenic species of Verticillium. Theseobservations suggest that VCP1 or similar enzyme(s) may play a role in the infection of invertebrates.

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Documento generato il 26/11/20 alle ore 13:31:07