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J. Biol. Chem., Vol. 277, Issue 35, 32133-32140, August 30, 2002

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Isolation, Characterization, and cDNA Sequence of a Carotenoid Binding Protein from the Silk Gland of Bombyx mori Larvae^*

Hiroko Tabunoki, Hiromu Sugiyama^§, Yoshiro Tanaka^¶, Hiroshi Fujii, Yutaka Banno, Zeina E. Jouni^**, Masahiko Kobayashi, Ryoichi Sato, Hideaki Maekawa^§§, and Kozo Tsuchida^§§¶¶

From  Bio-Application and System Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 183-0054, Japan, the ^§ Department of Parasitology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan, ^¶ Lion Corporation, Edogawa, Tokyo 132-0035, Japan, the  Center of Genetic Resources, University of Kyushu, Fukuoka 812-0053, Japan, the ^** Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona, 85721, the  Department of Agrobiology, University of Tokyo, Bunkyo, Tokyo 113-8657, Japan, and the ^§§ Department of Radiological Protection, National Institute of Infectious Diseases, Shinjuku, Tokyo 162-8640, Japan

A carotenoid binding protein (CBP) has been isolated from the silk glands of Bombyx mori larvae. The protein has an apparent molecular mass of 33 kDa and binds carotenoids in a 1:1 molar ratio. Lutein accounts for 90% of the bound carotenoids, whereas -carotene and -carotene are minor components. Immunological analysis demonstrated the presence of CBP only in the yellow-colored tissues of the silk gland, midgut, testis, and ovary. Several phenotypes of B. mori mutants linked to carotenoid transport have been utilized to characterize CBP. The Y (yellow hemolymph) gene controls uptake of carotenoids from the midgut lumen into the midgut epithelium, and larvae with the +^Y gene lack this property. Immunoblotting analysis confirmed the presence of CBP in mutants with the dominant Y gene only. Immunohistochemistry verified the localization of CBP in the villi of the midgut epithelium, indicating that CBP might be involved in absorption of carotenoids. A cDNA clone for CBP encoding a protein of 297 amino acids has been isolated from the B. mori silk gland cDNA library. The deduced amino acid sequence revealed that CBP is a novel member of the steroidogenic acute regulatory (StAR) protein family with its unique structural feature of a StAR-related lipid transfer domain, known to aid in lipid transfer and recognition. Lutein-binding capacity of the recombinant CBP (rCBP) determined by incubating rCBP with lutein followed by immunoprecipitation using anti-CBP IgG conjugated to protein A-Sepharose, demonstrated the formation of a lutein-rCBP complex. Sequence analyses coupled with binding specificity suggest that CBP is a new member of the StAR protein family that binds carotenoids rather than cholesterol.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AF309498.

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