Mollusc Crystallins: Physical and Chemical Properties and Phylogenetic Analysis

Abstract

The purpose of the present study was to perform bioinformatic analysis of crystallin diversity in aquatic molluscs based on the sequences in the NCBI Protein database. The objectives were as follows: (1) analysis of some physical and chemical properties of mollusc crystallins, (2) comparison of mollusc crystallins with zebrafish and cubomedusa Tripedalia cystophora crystallins, and (3) determination of the most probable candidates for the role of gastropod eye crystallins. The calculated average GRAVY values revealed that the majority of the seven crystallin groups, except for μ- and ζ-crystallins, were hydrophilic proteins. The predominant predicted secondary structures of the crystallins in most cases were α-helices and coils. The highest values of refractive index increment (dn/dc) were typical for crystallins of aquatic organisms with known lens protein composition (zebrafish, cubomedusa, and octopuses) and for S-crystallin of Pomacea canaliculata. The evolutionary relationships between the studied crystallins, obtained from multiple sequence alignments using Clustal Omega and MUSCLE, and the normalized conservation index, calculated by Mirny, showed that the most conservative proteins were Ω-crystallins but the most diverse were S-crystallins. The phylogenetic analysis of crystallin was generally consistent with modern mollusc taxonomy. Thus, α- and S-, and, possibly, J1A-crystallins, can be assumed to be the most likely candidates for the role of gastropod lens crystallins.