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Solution Structure of the Silkworm βGRP/GNBP3 N-Terminal Domain Reveals the Mechanism for β-1,3-Glucan-Specific Recognition
Kiyohiro Takahasi, Masanori Ochiai, Masataka Horiuchi, Hiroyuki Kumeta, Kenji Ogura, Masaaki Ashida, Fuyuhiko Inagaki and John H. Law
Proceedings of the National Academy of Sciences of the United States of America
Vol. 106, No. 28 (Jul. 14, 2009), pp. 11679-11684
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/40484010
Page Count: 6
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The β-1,3-glucan recognition protein (βGRP)/Gram-negative bacteriabinding protein 3 (GNBP3) is a crucial pattern-recognition receptor that specifically binds β-1,3-glucan, a component of fungal cell walls. It evokes innate immunity against fungi through activation of the prophenoloxidase (proPO) cascade and Toll pathway in invertebrates. The βGRP consists of an N-terminal β-1,3-glucan-recognition domain and a C-terminal glucanase-like domain, with the former reported to be responsible for the proPO cascade activation. This report shows the solution structure of the N-terminal β-1,3-glucan recognition domain of silkworm βGRP. Although the N-terminal domain of βGRP has a 0-sandwich fold, often seen in carbohydrate-binding modules, both NMR titration experiments and mutational analysis showed that βGRP has a binding mechanism which is distinct from those observed in previously reported carbohydarate-binding domains. Our results suggest that βGRP is a β-1,3-glucan-recognition protein that specifically recognizes a triple-helical structure of β-1,3-glucan.
Proceedings of the National Academy of Sciences of the United States of America © 2009 National Academy of Sciences