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Journal of Zhejiang University SCIENCE B 2009 Vol.10 No.6 P.434~444


MoFLP1, encoding a novel fungal fasciclin-like protein, is involved in conidiation and pathogenicity in Magnaporthe oryzae

Author(s):  Tong-bao LIU, Guo-qing CHEN, Hang MIN, Fu-cheng LIN

Affiliation(s):  State Key Laboratory for Rice Biology, Biotechnology Institute, Zhejiang University, Hangzhou 310029, China; more

Corresponding email(s):   fuchenglin@zju.edu.cn

Key Words:  Magnaporthe oryzae, Fasciclin, MoFLP1, Cellular localization, Conidiation, Pathogenicity

Tong-bao LIU, Guo-qing CHEN, Hang MIN, Fu-cheng LIN. MoFLP1, encoding a novel fungal fasciclin-like protein, is involved in conidiation and pathogenicity in Magnaporthe oryzae[J]. Journal of Zhejiang University Science B, 2009, 10(6): 434~444.

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author="Tong-bao LIU, Guo-qing CHEN, Hang MIN, Fu-cheng LIN",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T MoFLP1, encoding a novel fungal fasciclin-like protein, is involved in conidiation and pathogenicity in Magnaporthe oryzae
%A Tong-bao LIU
%A Guo-qing CHEN
%A Hang MIN
%A Fu-cheng LIN
%J Journal of Zhejiang University SCIENCE B
%V 10
%N 6
%P 434~444
%@ 1673-1581
%D 2009
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B0920017

T1 - MoFLP1, encoding a novel fungal fasciclin-like protein, is involved in conidiation and pathogenicity in Magnaporthe oryzae
A1 - Tong-bao LIU
A1 - Guo-qing CHEN
A1 - Hang MIN
A1 - Fu-cheng LIN
J0 - Journal of Zhejiang University Science B
VL - 10
IS - 6
SP - 434
EP - 444
%@ 1673-1581
Y1 - 2009
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B0920017

fasciclin family proteins have been identified as cell adhesion molecules in various organisms. In this study, a novel Magnaporthe oryzae fasciclin-like protein encoding gene, named MoFLP1, was isolated from a subtractive suppressive cDNA library and functionally analyzed. Sequence analysis showed that the MoFLP1 gene contains an open reading frame (ORF) of 1050 nucleotides encoding 349 amino acids with a calculated molecular weight of 35.85 kDa and a pI of 7.76. The deduced MoFLP1 protein contains a 17-amino acid secretion signal sequence and an 18-amino acid sequence with the characteristics of a glycosylphosphotidylinositol (GPI) anchor additional signal at its N- and C-terminuses, respectively. Potential N-glycosylation sites and domains involving cell adhesion were also identified in MoFLP1. Sequence analysis and subcellular localization by the expression of MoFLP1-GFP fusion construct in M. oryzae indicated that the MoFLP1 protein is probably localized on the vacuole membrane. Two MoFLP1 null mutants generated by targeted gene disruption exhibited marked reduction of conidiation, conidial adhesion, appressorium turgor, and pathogenicity. Our results indicate that fasciclin proteins play important roles in fungal development and pathogenicity in M. oryzae.

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article


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