Vertebrate-like betagamma-crystallins in the ocular lenses of a copepod.

The diverse crystallins are water-soluble proteins that are responsible for the optical properties of cellular lenses of animal eyes. While all vertebrate lenses contain physiological stress-related alpha- and betagamma-crystallins, some also contain taxon-specific, often enzyme-related crystallins. To date, the alpha- and betagamma-crystallins have been found only in vertebrate lenses. Here we report lenses from an invertebrate, the pontellid copepod Anomalocera ornata, accumulate betagamma-crystallin family members as judged by immunocytochemistry, western immunoblotting and microsequencing. Our data provide the first example of betagamma-crystallin members in an invertebrate lens, establishing that the use of this protein family as lens crystallins is not confined to vertebrates.