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The major advance during the past year was the identification of ligands for two of the previously known position-specific integrins in Drosophila. At the same time, two new Drosophila integrin subunits (one alpha and one beta) were discovered, and significant progress was made on developmental genetic analyses of integrin functions, shedding light on the roles of integrins in Drosophila development.

EBNA-1 is a nuclear antigen of lymphocytes infected by Epstein-Barr virus and whose size polymorphism correlates only with the strain of infecting virus and the length of the glycine-alanine copolymer encoded by the third internal repeat of the viral genome. The major antigenic determinant(s) also appear to reside in this region. We have been able to obtain efficient expression of this nuclear antigen in cultured Drosophila cells transfected with a cosmid carrying the EBNA-1 coding region, indicating that insect mechanisms recognise control sequences and transcripts of the herpes virus. The association of a vimertin-like protein of mol. wt. 46,000 with Drosophila cell nuclei has been found to vary with culture conditions and heat shock. We now find that the level and nuclear association of this protein also increase after transfection with either EBNA-1 or yolk protein DNA.

DNA-mediated cotransformation has been used to transfer a Drosophila melanogaster heat shock locus into cultured Drosophila hydei cells by use of the copia-based selectable vector pCV2gpt and of pMH10A, a cloned 87A7 heat shock locus encoding a mutant heat shock protein (hsp). Transformed lines contain between 50 and 200 copies of both plasmids, each separately organized as a head-to-tail concatemer which is stably maintained in the transformed lines. Exposure of the cotransformants to heat shock temperatures induces the regulated expression of the hsp RNA and the mutant hsp in all the lines analyzed.