Journal Article

Structural Divergence of Cysteine-Rich Secretory Proteins in Snake Venoms

Yukiko Matsunaga, Yasuo Yamazaki, Fumiko Hyodo, Yusuke Sugiyama, Masatoshi Nozaki and Takashi Morita

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 145, issue 3, pages 365-375
Published in print March 2009 | ISSN: 0021-924X
Published online December 2008 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/jb/mvn174
Structural Divergence of Cysteine-Rich Secretory Proteins in Snake Venoms

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Cysteine-rich secretory proteins (CRISPs) are expressed in spermatocytes and granules of neutrophils in mammals, and are associated with sperm maturation and host defense. Related proteins have recently been recovered in snake venoms, and some of the snake venom-derived CRISPs exhibit ion channel blocking activity. Here we isolated and identified two novel CRISPs (kaouthin-1 and kaouthin-2) from the venom of Naja kaouthia (Elapidae), and cloned the encoding cDNAs. Kaouthin-1 and kaouthin-2 were classified into two broad sister groups of Elapidae, the Asian species and the marine/Australian species, respectively. Sequence comparisons reveal that the high-frequency variable regions among snake venom CRISPs define a continuous line on the molecular surface of the N-terminal pathogenesis-related protein-1 (PR-1) domain and the C-terminal cysteine-rich domain (CRD). Snake venom proteins generally display efficient molecular diversity around functionally key regions, suggesting that the PR-1 domain of CRISPs is important for the recognition of target molecules.

Keywords: CRISP; Naja kaouthia; pathogenesis-related protein; cysteine-rich domain; ion channel

Journal Article.  5129 words.  Illustrated.

Subjects: Biochemistry

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