Characterization of a myosin heavy chain gene from Brugia malayi.
We have previously shown that an antigen recognized by antibodies in sera of several microfilaremic individuals from a Wuchereria bancrofti endemic area bears strong homology to an invertebrate muscle protein. We have cloned and sequenced the entire gene containing this antigen encoding fragment and present data that confirms that the antigen is myosin heavy chain (MHC). This gene, which we have named Bmmyo-1 extends over 11 kb and has the potential to encode a protein of 1957 amino acids. The coding sequence is interrupted by 14 introns, most of which are larger than those in the myosin gene of the free-living nematode, Caenorhabditis elegans. The protein encoded by this gene bears greatest homology (75.1% identity) to the C. elegans myosin isoform MHC-B, encoded by the unc-54 gene. MHC-B is the major body wall myosin in C. elegans.
Werner
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Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY.
Rajan
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D000595:Amino Acid Sequence; D000818:Animals; D000947:Antigens, Helminth / Q000235:genetics; D001483:Base Sequence; D002009:Brugia / Q000235:genetics*; D002107:Caenorhabditis / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005091:Exons; D015698:Genomic Library; D007438:Introns; D008969:Molecular Sequence Data; D009218:Myosins / Q000235:genetics*; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D000947:Antigens, Helminth; D004247:DNA; D009218:Myosins