Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 90; no. 8; pp. 3569 - 3573
• Main Authors: Gmachl, M. (Austrian Academy of Sciences, Salzburg, Austria), Kreil, G
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 15.04.1993; National Acad Sciences; National Academy of Sciences
• Subjects: Acrosome - physiology; ADN; Amino Acid Sequence; Amino acids; Analytical, structural and metabolic biochemistry; Animals; APIS MELLIFERA; Base Sequence; Bee Venoms; Bees; Biochemistry; Biological and medical sciences; cDNA; Cell Membrane - chemistry; CLONE; CLONES; Cloning, Molecular; CODE GENETIQUE; CODIGO GENETICO; Complementary DNA; DNA; DNA - genetics; DNA - isolation & purification; Enzymes; Enzymes and enzyme inhibitors; Escherichia coli - genetics; ESPERMATOZOO; EXPRESION GENICA; EXPRESSION DES GENES; Female; Fundamental and applied biological sciences. Psychology; Gene Library; genes; GLANDE ANIMALE; GLANDULAS ANIMALES; GLICOSIDASAS; GLYCOSIDASE; Guinea Pigs; homology; hyaluronidase; Hyaluronoglucosaminidase - chemistry; Hyaluronoglucosaminidase - genetics; Hydrolases; Insect genetics; Insect reproduction; Male; MAMIFEROS; Mammals; MAMMIFERE; Membrane Proteins - chemistry; Membrane Proteins - genetics; Molecular Sequence Data; nucleotide sequence; Oligodeoxyribonucleotides; PH-20 protein; predictions; Proteins; RNA; RNA - genetics; RNA - isolation & purification; RNA, Messenger - analysis; RNA, Messenger - metabolism; SECUENCIA NUCLEICA; Sequence Homology, Amino Acid; SEQUENCE NUCLEIQUE; Spermatozoa; Spermatozoa - physiology; SPERMATOZOIDE; Testis - physiology; TOXINAS; TOXINE; VENENOS; VENIN; Venoms; Hyaluronidase; Membrane protein; Spermatozoa; Enzyme; Insecta; Rodentia; Apidae; Homology; Primary structure; Apis mellifera; Vertebrata; Mammalia; Apoidea; Arthropoda; Venom; Hymenoptera; Invertebrata; Molecular cloning; Hamster; Aculeata
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.90.8.3569

The venom of honeybees, Apis mellifera, contains several biologically active peptides and two enzymes, one of which is a hyaluronidase. By using degenerate oligonucleotides derived from the amino-terminal sequence of this hyaluronidase reported by others, clones encoding the precursor for this enzyme could be isolated from a cDNA library prepared from venom glands of worker bees. The deduced amino acid sequence showed that bee venom hyaluronidase is a polypeptide composed of 349 amino acids containing four cysteines and three potential sites for N-glycosylation. The sequence of the precursor also indicated that the conversion of the pro-enzyme to the end product must involve cleavage of a Thr-Pro bond, a most unusual processing reaction. The mRNA encoding hyaluronidase could also be detected in testes from drones. Expression of the cloned cDNA in Escherichia coli yielded a 41-kDa polypeptide that had hyaluronidase activity. Interestingly, the hyaluronidase from bee venom glands exhibited significant homology to PH-20, a membrane protein of guinea pig sperm involved in sperm-egg adhesion. These structural data support the long-held view that hyaluronidases play a role in fertilization.