Invertebrates glycosylation

Wilson IBH. Glycosylation of proteins in plants and invertebrates. Curr. Opin. Struct. Biol. 2002 12 569-577. 

The glycosyltransferase which glycosylates the hydroxyl group of 5-hydroxylysine in collagens and similar proteins appears to recognize the amino acid sequence -G1 y-X—HyZ-Gly-Y-Arg- Whereas the amino acids X and Y are quite variable, the positions of Gly, Hyl, and Arg are invariant in the glycopeptides of ten vertebrate and invertebrate collagens (169). 

Flaviviruses are small, enveloped viruses, with cubic symmetry, approximately 45 nm in diameter, which replicate in vertebrate and invertebrate cells. The nucleocapsid contains the single-stranded plus RNA associated with a nucleocapsid protein, C, which has a molecular weight of 13K. The viral envelope consists of one large glycoprotein, E, of molecular weight approximately 55K, and a small 8K membrane-associated protein, M, which is not glycosylated (Wes-taway, 1980 Matthews, 1982). The structural components of flaviviruses have been reviewed by Russell et al. (1980) and the replication strategy of these viruses reviewed by Westaway (1980). 

In humans, such glycoconjugates are involved in the post-translational modification of proteins, but this is usually achieved by the formation of an O- or N-glycosyla-ted derivative. It was not until recently that C-glycosylated derivatives were shown to be involved in the metabolism of tryptophan, and the presence of such glycoconjugates in three species of ascidians implies the existence of a C-mannosyltransferase in these invertebrates, which may become a new source of C-glycoconjugates (see above and Carcia et al, 2000). 

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