title: Influenza A virus-binding activity of glycoglycerolipids of aquatic bacteria.
abstract: As the aqueous sphere has been proposed to be an important source medium for the virus infection of land animals, the glycolipids of some aquatic organisms were examined for human influenza A virus-binding activity. Active compounds were not found among the eight echinoderm gangliosides, but two active non-sialylated glycoglycerolipids were isolated from an aquatic bacterium, Corynebacterium aquaticum. The structural formula of one of them, H632A, was elucidated to be 1-14-methyl-hexadecanoyl-3-alpha-D-galactopyranosyl-(1-->3)-6-(12-met hyl-tetradecanoyl)-1-alpha-D-mannopyranosyl]-sn-glycerol. The latter together with reported one elsewhere, S365A, 1-14-methyl-hexadecanoyl-3-[alpha-D-mannopyranosyl-(1-->3)-6-(12-meth yl-tetradecanoyl)-1-alpha-D-mannopyranosyl]-sn-glycerol, apparently bound to three human influenza viruses, A/PR/8/34 (H1N1), A/Aichi/2/68 (H3N2), and A/Memphis/1/71 (H3N2), exhibiting 7-12% (H632A) and 10-22% (S365A) of the activities of the control substances (Neu5Acalpha2-3-paragloboside and Neu5Acalpha2-6- paragloboside). Additionally, these glycolipids were assumed to have virus-neutralizing activities for the following two reasons: (i) The hemagglutination and hemolysis activities of the viruses were inhibited by the glycolipid. (ii) The leakage of a cytosolic enzyme (lactate dehydrogenase) from Madin-Darby canine kidney cells on virus infection was prevented by the glycolipids to nearly the same extent as by fetuin. This is the first evidence of the binding- and neutralizing-abilities of native glycoglycerolipids as to influenza viruses.
authors.affiliation: Central Research Laboratories, Mercian Corporation, Johnan, Fujisawa 251-0057, Japan. knakata@mb.infoweb.ne.jp.
authors.forename: K
authors.initials: K
authors.lastname: Nakata
authors.forename: C T
authors.initials: CT
authors.lastname: Guo
authors.forename: M
authors.initials: M
authors.lastname: Matsufuji
authors.forename: A
authors.initials: A
authors.lastname: Yoshimoto
authors.forename: M
authors.initials: M
authors.lastname: Inagaki
authors.forename: R
authors.initials: R
authors.lastname: Higuchi
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
mesh_terms: D000818:Animals; D001419:Bacteria / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D002240:Carbohydrate Sequence; D002460:Cell Line; D003352:Corynebacterium / Q000737:chemistry / Q000145:classification / Q000378:metabolism; D004285:Dogs; D006017:Glycolipids / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D006386:Hemagglutination Tests; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D009980:Influenza A virus / Q000378:metabolism*; D007668:Kidney / Q000166:cytology / Q000187:drug effects / Q000821:virology; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008969:Molecular Sequence Data; D015394:Molecular Structure; D014871:Water Microbiology
chemical_list: D006017:Glycolipids; D007770:L-Lactate Dehydrogenase