LITOMOSOIDES-CARINII MICROFILARIAL SHEATHS - PARTIAL AMINO-ACID-SEQUENCES OF SEVERAL MAJOR POLYPEPTIDE CONSTITUENTS

Isolated sheaths from Litomosoides carinii microfilariae were disinteg rated by reduction with dithiothreitol and were C-14-carboxymethylated . Five major sheath proteins thus solubilized were purified by size ex clusion chromatography and reversed-phase HPLC (rpHPLC). Proteolytic f ragments of complete sheaths and of the single sheath proteins were is olated by rpHPLC and were N-terminally sequenced. a library of 27 part ial sheath polypeptide sequences was thus established, 21 of which cou ld be assigned to three L. carinii sheath structural genes (shp1,2, an d 3/3a) isolated on the basis of this and of previous amino acid seque nce information. The remaining peptides document the presence of at le ast one additional major sheath constituent.