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Literature DB >> 8240010

The porcine paramyxovirus LPM specifically recognizes sialyl (alpha 2,3) lactose-containing structures.

J Reyes-Leyva¹, P Hernández-Jáuregui, L F Montaño, E Zenteno.

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.

Entities: Chemical

Mesh：

Substances：

Year: 1993 PMID： 8240010 DOI： 10.1007/bf01309755

Source DB: PubMed Journal: Arch Virol ISSN： 0304-8608 Impact factor: 2.574

13 in total

1. Identification of the porcine paramyxovirus LPMV matrix protein gene: comparative sequence analysis with other paramyxoviruses.

Authors: M Berg; A Sundqvist; J Moreno-López; T Linné
Journal: J Gen Virol Date: 1991-05 Impact factor: 3.891

2. Encephalomyelitis, reproductive failure and corneal opacity (blue eye) in pigs, associated with a paramyxovirus infection.

Authors: H A Stephan; G M Gay; T C Ramírez
Journal: Vet Rec Date: 1988-01-02 Impact factor: 2.695

3. The haemagglutinin-neuraminidase glycoprotein of the porcine paramyxovirus LPMV: comparison with other paramyxoviruses revealed the closest relationship to simian virus 5 and mumps virus.

Authors: A Sundqvist; M Berg; J Moreno-López; T Linné
Journal: Arch Virol Date: 1992 Impact factor: 2.574

4. The structural proteins of a porcine paramyxovirus (LPMV).

Authors: A Sundqvist; M Berg; P Hernandez-Jauregui; T Linné; J Moreno-López
Journal: J Gen Virol Date: 1990-03 Impact factor: 3.891

5. Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharides of poly-N-acetyllactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium.

Authors: R W Loveless; T Feizi
Journal: Infect Immun Date: 1989-04 Impact factor: 3.441

6. The P gene of the porcine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited.

Authors: M Berg; B Hjertner; J Moreno-López; T Linné
Journal: J Gen Virol Date: 1992-05 Impact factor: 3.891

The porcine paramyxovirus LPM specifically recognizes sialyl (alpha 2,3) lactose-containing structures.

1. Identification of the porcine paramyxovirus LPMV matrix protein gene: comparative sequence analysis with other paramyxoviruses.

2. Encephalomyelitis, reproductive failure and corneal opacity (blue eye) in pigs, associated with a paramyxovirus infection.

3. The haemagglutinin-neuraminidase glycoprotein of the porcine paramyxovirus LPMV: comparison with other paramyxoviruses revealed the closest relationship to simian virus 5 and mumps virus.

4. The structural proteins of a porcine paramyxovirus (LPMV).

5. Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharides of poly-N-acetyllactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium.

6. The P gene of the porcine paramyxovirus LPMV encodes three possible polypeptides P, V and C: the P protein mRNA is edited.

7. Characterization of a paramyxovirus isolated from the brain of a piglet in Mexico.

Review 8. Chemistry, metabolism, and biological functions of sialic acids.

9. Receptor ganglioside content of three hosts for Sendai virus. MDBK, HeLa, and MDCK cells.

10. Spatial conformation of glycans and glycoproteins.

1. Purification and characterization of the hemagglutinin-neuraminidase of Porcine rubulavirus LPMV.

Review 2. Sialic acids in molecular and cellular interactions.

3. Differential expression of sialic acid on porcine organs during the maturation process.

4. Transcription of interferon stimulated genes in response to Porcine rubulavirus infection in vitro.