The influenza viruses have the ability to agglutinate erythrocytes by binding to sialic acid receptors on the host cell. Human influenza viruses preferentially bind to sialic acid linked to galactose by α 2.6 linkage, while avian influenza viruses preferentially bind to sialic acid linked to Gal by α 2.3 linkage. There is a close correlation between the ability of influenza A viruses to agglutinate erythrocytes from different animal species and their receptor specificity. The haemagglutination and haemagglutination inhibition assays are influenced by the species of erythrocytes. To provide an overview of the expression of sialic acid receptors on different erythrocytes, avian (turkey, chicken, pigeon) and mammalian (sheep, horse, human) species have been analysed by flow cytometry. Chicken, turkey and human erythrocytes display both types of linkages. Horse and sheep erythrocytes show almost exclusively α 2.3 Gal linkages, while pigeon erythrocytes express almost exclusively α 2.6 Gal linkages. The erythrocytes from the same avian and mammalian species have been evaluated by haemagglutination and haemagglutination inhibition assays with seasonal and avian strains. Chicken and turkey erythrocytes seem to be the most appropriate for both assays with seasonal influenza strains, in addition to pigeon erythrocytes, particularly for the B strains. In the case of the avian strain, chicken erythrocytes are suitable for haemagglutination assay and horse erythrocytes for haemagglutination inhibition assay. The choice of erythrocytes has a significant impact on the titres measured by both assays.

Trombetta, C.M., Ulivieri, C., Cox, R.J., Remarque, E.J., Centi, C., Perini, D., et al. (2018). Impact of erythrocyte species on assays for influenza serology. JOURNAL OF PREVENTIVE MEDICINE AND HYGIENE, 59(1), E1-E7 [10.15167/2421-4248/jpmh2018.59.1.870].

Impact of erythrocyte species on assays for influenza serology

Trombetta, C. M.
;
Ulivieri, C.;Rossi, S.;Marchi, S.;Montomoli, E.
2018-01-01

Abstract

The influenza viruses have the ability to agglutinate erythrocytes by binding to sialic acid receptors on the host cell. Human influenza viruses preferentially bind to sialic acid linked to galactose by α 2.6 linkage, while avian influenza viruses preferentially bind to sialic acid linked to Gal by α 2.3 linkage. There is a close correlation between the ability of influenza A viruses to agglutinate erythrocytes from different animal species and their receptor specificity. The haemagglutination and haemagglutination inhibition assays are influenced by the species of erythrocytes. To provide an overview of the expression of sialic acid receptors on different erythrocytes, avian (turkey, chicken, pigeon) and mammalian (sheep, horse, human) species have been analysed by flow cytometry. Chicken, turkey and human erythrocytes display both types of linkages. Horse and sheep erythrocytes show almost exclusively α 2.3 Gal linkages, while pigeon erythrocytes express almost exclusively α 2.6 Gal linkages. The erythrocytes from the same avian and mammalian species have been evaluated by haemagglutination and haemagglutination inhibition assays with seasonal and avian strains. Chicken and turkey erythrocytes seem to be the most appropriate for both assays with seasonal influenza strains, in addition to pigeon erythrocytes, particularly for the B strains. In the case of the avian strain, chicken erythrocytes are suitable for haemagglutination assay and horse erythrocytes for haemagglutination inhibition assay. The choice of erythrocytes has a significant impact on the titres measured by both assays.
Trombetta, C.M., Ulivieri, C., Cox, R.J., Remarque, E.J., Centi, C., Perini, D., et al. (2018). Impact of erythrocyte species on assays for influenza serology. JOURNAL OF PREVENTIVE MEDICINE AND HYGIENE, 59(1), E1-E7 [10.15167/2421-4248/jpmh2018.59.1.870].
File in questo prodotto:
File Dimensione Formato  
076_2018_JPMH-Trombetta.pdf

accesso aperto

Tipologia: PDF editoriale
Licenza: PUBBLICO - Pubblico con Copyright
Dimensione 222.65 kB
Formato Adobe PDF
222.65 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/1059302