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Purification and Characterization of AAVP

Purification and
Characterization of AAVP, a Protein Inhibitor of TMV Infection, from the Edible
Fungus, Agrocybe
aegerita

SUN Hui, WU Zu-Jian, XIE Lian-Hui* , LIN Qi-Ying
( Institute of Plant Virology, Fujian Agriculture University, Fuzhou 350002,
China
)

Abstract    A protein
with activity of inhibiting TMV infection on Nicotiana glutinosa,
named AAVP, was isolated and purified from the fruiting bodies of edible fungus
Agrocybe aegerita by precipitation of 40%–80% saturation of (NH4)2SO4
followed by DEAE-Fast Flow and S-200 column chromatography. The protein was
proved to be homogeneous by SDS-PAGE and IEF. Analysis of the composition of
amino acids showed that this protein contained no cysteine, poor in methionine
and phenylalanine and rich in acidic and hydroxyl amino acids. The inhibition
of TMV was 84.32% when the concentration of AAVP was 200 mg/L. N-terminus of
this protein was blocked by pyroglutamyl, and the N-terminal sequence was
QGVNIYNIVAGA. On potato-sucrose-agar medium, the purified protein did not
inhibit the growth of three plant pathogen fungi, Trichoderma viride,
Colletotrichum musae
and Fusarium oxysporum.
Key words    antiphytoviral protein
purification characterization

*Corresponding author Tel/Fax, 86-591-3744704 e-mail, [email protected]