title: The porcine paramyxovirus LPM specifically recognizes sialyl (alpha 2,3) lactose-containing structures.
abstract: The porcine paramyxovirus LPM recognizes alpha, but not beta, anomers of sialic acid containing structures, specifically sialyl (alpha 2,3) lactose. The virus specificity is directed to the sialyl residue and to the C'4 axial OH and the C'6 CH2OH of the galactose present in this structure.
authors.affiliation: Depto. Bioquímica, Fac. Medicina, Universidad Nacional Autónoma de México, México.
authors.forename: J
authors.initials: J
authors.lastname: Reyes-Leyva
authors.forename: P
authors.initials: P
authors.lastname: Hernández-Jáuregui
authors.forename: L F
authors.initials: LF
authors.lastname: Montaño
authors.forename: E
authors.initials: E
authors.lastname: Zenteno
mesh_terms: D000372:Agglutination Tests; D000818:Animals; D002240:Carbohydrate Sequence; D015726:Giant Cells / Q000166:cytology; D006801:Humans; D007785:Lactose / Q000031:analogs & derivatives* / Q000378:metabolism; D008969:Molecular Sequence Data; D010252:Paramyxoviridae / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D013552:Swine / Q000382:microbiology; D014709:Vero Cells
chemical_list: D011991:Receptors, Virus; D012794:Sialic Acids; C000020:N-acetylneuraminoyllactose; D007785:Lactose