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Volume 272, Number 44, Issue of October 31, 1997 pp. 27839-27847
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Main Protein of the Aggregation Factor Responsible for Species-specific Cell Adhesion in the Marine Sponge Microciona prolifera Is Highly Polymorphic

(Received for publication, June 12, 1997)

From the Friedrich Miescher-Institut, P.O. Box 2543, CH-4002 Basel, Switzerland and the Marine Biological Laboratory, Woods Hole, Massachusetts 02543

Species-specific cell recognition in sponges, the oldest living metazoans, is based on a proteoglycan-like aggregation factor. We have screened individual sponge cDNA libraries, identifying multiple related forms for the aggregation factor core protein (MAFp3). Northern blots show the presence in several human tissues of transcripts strongly binding a MAFp3-specific probe. The open reading frame for MAFp3 is not interrupted in the 5 direction, revealing variable protein sequences that contain numerous introns equally spaced. We have studied tissue histocompatibility within a sponge population, finding 100% correlation between rejection behavior and the individual-specific restriction fragment length polymorphism pattern using aggregation factor-related probes. PCR amplifications with specific primers showed that at least some of the MAFp3 forms are allelic and distribute in the population used. A pronounced polymorphism is also observed when analyzing purified aggregation factor in polyacrylamide gels. Protease digestion of the polymorphic glycosaminoglycan-containing bands indicates that glycans are also responsible for the variability. The data presented reveal a high polymorphism of aggregation factor components, which matches the elevated sponge alloincompatibility, suggesting an involvement of the cell adhesion system in sponge allogeneic reactions.

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