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A Single Amino Acid Substitution in the Bombyx-specific Mucin-Like Membrane Protein Causes Resistance to Bombyx Mori Densovirus

Katsuhiko Ito, Kurako Kidokoro, Susumu Katsuma, Hideki Sezutsu, Keiro Uchino, Isao Kobayashi, Toshiki Tamura, Kimiko Yamamoto, Kazuei Mita, Toru Shimada, Keiko Kadono-Okuda

Sci Rep. 2018 May 9;8(1):7430.

PMID: 29743532

Abstract:

Bombyx mori densovirus type 1 (BmDV) is a pathogen that causes flacherie disease in the silkworm. The absolute nonsusceptibility to BmDV among certain silkworm strains is determined independently by two genes, nsd-1 and Nid-1. However, neither of these genes has been molecularly identified to date. Here, we isolated the nsd-1 gene by positional cloning and characterized the properties of its product, NSD-1. Sequence and biochemical analyses revealed that this gene encodes a Bombyx-specific mucin-like glycoprotein with a single transmembrane domain. The NSD-1 protein was specifically expressed in the larval midgut epithelium, the known infection site of BmDV. Sequence analysis of the nsd-1 gene from 13 resistant and 12 susceptible strains suggested that a specific arginine residue in the extracellular tail of the NSD-1 protein was common among susceptible strains. Germline transformation of the susceptible-type nsd-1 (with a single nucleotide substitution) conferred partial susceptibility to resistant larvae, indicating that the + nsd-1 gene is required for the susceptibility of B. mori larvae to BmDV and the susceptibility is solely a result of the substitution of a single amino acid with arginine. Taken together, our results provide striking evidence that a novel membrane-bound mucin-like protein functions as a cell-surface receptor for a densovirus.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP476316582 NID-1 NID-1 476316-58-2 Price
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