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CHARACTERIZATION OF A LIBRARY OF MONOCLONAL ANTIBODIES AGAINST VITELLOGENIN: CONSERVATION OF EPITOPES
Citation:
Denslow, N D., L. Green, M. M. Chow, S. A. Heppell, L C. Folmar, AND C. V. Sullivan. CHARACTERIZATION OF A LIBRARY OF MONOCLONAL ANTIBODIES AGAINST VITELLOGENIN: CONSERVATION OF EPITOPES. Presented at Second SETAC World Congress (16th Annual Meeting), Vancouver, BC, CANADA, November 05 - 09, 1995.
Impact/Purpose:
Presentation
Description:
The egg yolk precursor, vitellogenin, a complex phospho-lipo-glycoprotein, is the main source of nutrients for the developing embryo of all oviparous animals. Because of this role it has few evolutionary constraints imposed on its structure, varying widely among species. Despite the high degree of primary sequence variability, vitellogenins whose primary structures have been determined, do have a signature sequence and share spotty but significant stretches of similarity. This implies that some of these regions of high conservation may be necessary for the delivery of vitellogenin to growing oocytes or its function in eggs and embryos. We have prepared a panel of monoclonal antibodies against several different fish vitellogenins, each recognizing a specific epitope. Some of the monoclonal antibodies interact with vitellogenin from only one species, making them useful for species identification. Others interact widely with vitellogenins from different species suggesting that they recognize epitopes that may be relatively well conserved. One of our antibodies, IgM HL976, cross-reacts with all vertebrate vitellogenins tested to date, suggesting that this epitope is conserved in vitellogenins spanning a large separation in evolutionary time from birds to reptiles to amphibians to fishes.