Structure-Function Analysis of a CVNH-LysM Lectin Expressed during Plant Infection by the Rice Blast Fungus Magnaporthe oryzae

被引:42
作者
Koharudin, Leonardus M. I. [2 ]
Viscomi, Arturo R. [1 ]
Montanini, Barbara [1 ]
Kershaw, Michael J. [3 ]
Talbot, Nicholas J. [3 ]
Ottonello, Simone [1 ]
Gronenborn, Angela M. [2 ]
机构
[1] Univ Parma, Dipartimento Biochim Biol Mol, I-43100 Parma, Italy
[2] Univ Pittsburgh, Sch Med, Dept Biol Struct, Pittsburgh, PA 15260 USA
[3] Univ Exeter, Sch Biosci, Exeter EX4 4QD, Devon, England
基金
美国国家卫生研究院;
关键词
PROTEIN CYANOVIRIN-N; INACTIVATING PROTEIN; CRYSTAL-STRUCTURES; BINDING; MUTANT; DOMAIN; VISUALIZATION; STABILITY; HOMOLOGS; REVEALS;
D O I
10.1016/j.str.2011.03.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The rice blast fungus Magnaporthe oryzae's genome encodes a hypothetical protein (MGG_03307) containing a type III CVNH lectin, in which a LysM domain is inserted between individual repeats of a single CVNH domain. At present, no structural or ligand binding data are available for any type Ill CVNH and functional studies in natural source organisms are scarce. Here, we report NMR solution structure and functional data on MGG_03307. The structure of the CVNH/LysM module revealed that intact and functionally competent CVNH and LysM domains are present. Using NMR titrations, carbohydrate specificities for both domains were determined, and it was found that each domain behaves as an isolated unit without any interdomain communication. Furthermore, live-cell imaging revealed a predominant localization of MGG_03307 within the appressorium, the specialized fungal cell for gaining entry into rice tissue. Our results suggest that MGG_03307 plays a role in the early stages of plant infection.
引用
收藏
页码:662 / 674
页数:13
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