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. 2013 Mar 1;288(9):6588. doi: 10.1074/jbc.A112.418012

A lectin from the mussel Mytilus galloprovincialis has a highly novel primary structure and induces glycan-mediated cytotoxicity of globotriaosylceramide-expressing lymphoma cells.

Yuki Fujii, Naoshi Dohmae, Koji Takio, Sarkar M A Kawsar, Ryo Matsumoto, Imtiaj Hasan, Yasuhiro Koide, Robert A Kanaly, Hidetaro Yasumitsu, Yukiko Ogawa, Shigeki Sugawara, Masahiro Hosono, Kazuo Nitta, Jiharu Hamako, Taei Matsui, Yasuhiro Ozeki
PMCID: PMC3585096

VOLUME 287 (2012) PAGES 44772–44783

As mentioned under the Introduction, Belogortseva et al. (Ref. 10 from our work) reported in 1998 a GalNAc/Gal-binding lectin isolated from Crenomytilus grayanus, a sea mussel related to the genus Mytilus. The primary structure of the lectin was not presented in the 1998 paper. While our paper was in press, we were informed that the mRNA sequence of the Crenomytilus lectin was submitted to GenBankTM by Kovalchuk et al. (Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of Russian Academy of Sciences, Vladivostok, Russia) and appeared on the website on January 30, 2012 (www.ncbi.nlm.nih.gov/nuccore/JQ314213.1).

This useful information led to the further online discovery of a deduced amino acid sequence coded by the mRNA sequence Mg_Nor01_51P18, which was submitted on February 10, 2009 to the GenBankTM (accession no. FL492661.1; www.ncbi.nlm.nih.gov/nucest/FL492661.1) as an mRNA coding an unknown protein by Bernante et al. (G. Lanfranchi's group, Department of Biology and CRIBI, Biotechnology Centre, University of Padova, Padova, Italy) from the EST database for Mytilus galloprovincialis, MytiBase (http://mussel.cribi.unipd.it; Ref. 2 of our work). The FL492661.1 sequence and its encoded protein have not been published to our knowledge. According to a “BlastX” search, the protein sequence deduced from the FL492661.1 mRNA sequence showed 100% identity with the primary structure of MytiLec (accession no. B3EWR1.1; http://www.ncbi.nlm.nih.gov/protein/410591642) and 88% homology with that of the Crenomytilus lectin.


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