Adaptive amino acid composition in collagens of parasitic nematodes

• Collagens of parasitic species showed decreased usage of the hydrophilic residues A, D, and Q.
• Collagens of parasitic species showed increased usage of the hydrophobic resides I, L, and M.
• This trend was seen in parasitic species of both the order Rhabdita and the order Spirurida.
• Hydrophobic amino acids reduced predicted propensity for B-cell epitope formation.
• Evasion of host immune responses may select for parasite collagen amino acid composition.

Amino acid composition was analyzed in the glycine-rich repeat region of 306 collagens belonging to three major families of collagens from both parasitic and free-living nematodes. The collagens of parasitic species showed a tendency toward decreased usage of the hydrophilic residues A, D, and Q and increased usage of the hydrophobic resides I, L, and M; and this trend was seen in parasitic species of both the order Rhabdita and the order Spirurida. The amino acid composition of collagens of parasitic Rhabdita thus tended to resemble those of Spirurida more than that of free-living Rhabdita, suggesting an association between amino acid composition and a parasitic lifestyle. Computer predictions suggested that the more hydrophobic amino acid composition was associated with a reduction of the propensity towards B-cell epitope formation, suggesting that evasion of host immune responses may be a major selective factor responsible for the parasite-specific trend in collagen amino acid composition.

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