Preparation of monoclonal antibodies for the diagnosis of influenza A infection using different immunization protocols

Varečková, E; Betáková, Tatiana; Mucha, V; Solariková, L; Kostolanský, F; Waris, Matti; Russ, G

doi:10.1016/0022-1759(94)00307-i

Cited by 41 publications

(21 citation statements)

References 14 publications

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“…(45). Based on phylogenetic analysis, these strains were selected from the major H5N1 clades in current circulation (clade 1, 2.1, 2.2, and 2.3) to cover the genetic and antigenic diversities of H5N1 viruses (8,41).…”

Section: Methodsmentioning

confidence: 99%

Antigenic Profile of Avian H5N1 Viruses in Asia from 2002 to 2007

Chen

Wang

et al. 2008

J Virol

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Antigenic profiles of post-2002 H5N1 viruses representing major genetic clades and various geographic sources were investigated using a panel of 17 monoclonal antibodies raised from five H5N1 strains. Four antigenic groups from seven clades of H5N1 virus were distinguished and characterized based on their cross-reactivity to the monoclonal antibodies in hemagglutination inhibition and cell-based neutralization assays. Genetic polymorphisms associated with the variation of antigenicity of H5N1 strains were identified and further verified in antigenic analysis with recombinant H5N1 viruses carrying specific mutations in the hemagglutinin protein. Modification of some of these genetic variations produced marked improvement to the immunogenicity and cross-reactivity of H5N1 strains in assays utilizing monoclonal antibodies and ferret antisera raised against clade 1 and 2 H5N1 viruses, suggesting that these sites represent antigenically significant amino acids. These results provide a comprehensive antigenic profile for H5N1 virus strains circulating in recent years and will facilitate the recognition of emerging antigenic variants of H5N1 virus and aid in the selection of vaccine strains.

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Section: Methodsmentioning

confidence: 99%

Antigenic Profile of Avian H5N1 Viruses in Asia from 2002 to 2007

Chen

Wang

et al. 2008

J Virol

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“…Intranasal administration of antigen without the use of adjuvant was performed. We did not investigate whether this immunization method is indeed superior to other methods used to induce cross-reactive antibodies [such as repeated administration of purified influenza virus, sequential infection or immunization with drift variants, use of (different) adjuvants or other routes of administration (Vareckova et al, 1995 ;Tamura et al, 1992Tamura et al, , 1994]. However, serum obtained just before fusion was highly cross-reactive, and supernatants of 15 of 32 polyclonal cell populations obtained after fusion showed cross-reactivity with A\Beijing\352\89 virus.…”

Section: Discussionmentioning

confidence: 99%

An antibody which binds to the membrane-proximal end of influenza virus haemagglutinin (H3 subtype) inhibits the low-pH-induced conformational change and cell-cell fusion but does not neutralize virus.

Vanlandschoot¹,

Beirnaert

Barrère³

et al. 1998

Journal of General Virology

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“…As a loading control, the detection of the β-actin was used by the mouse anti-β-actin monoclonal antibody (Sigma Aldrich). Monoclonal antibody (MAb) AG55 anti-PB1-F2 (Krejnusová et al, 2009) and MAb 107 anti-NP (Varečková et al, 1995) were prepared by the standard hybridoma procedure. MAb M21 anti-M1 and MAb NS1 anti-NS1 were kindly provided by John Yewdell, Bethesda, NIH.…”

Section: Cells and Viruses Madin-darby Canine Kidney Cells (Mdck)mentioning

confidence: 99%

N-terminal region of the PB1-F2 protein is responsible for increased expression of influenza A viral protein PB1

Košík¹,

Krejnusová²,

Bystrická³

et al. 2011

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Summary. -Influenza A virus (IAV) PB1-F2 protein is encoded by an alternative reading frame (+1) within the PB1 gene. PB1-F2 has been shown to contribute to the pathogenesis of influenza virus infection as well as to the secondary bacterial infection. More recently has been shown that PB1-F2 protein may regulate a viral RNA (vRNA) polymerase activity by the interaction with PB1 protein. We proved that PB1-F2 protein increased the level of expression of PB1 protein and vRNA in the infected cells. Moreover, we demonstrated that a higher level of vRNA expression resulted in the increase of expression of multiple viral proteins, including NP, M1, and NS1. Finally, we used plasmids expressing N-terminal (1-50 aa) or C-terminal (51-87 aa) region of the PB1-F2 molecule for transfection of MDCK cells co-infected with influenza A/Puerto Rico/8/34 (H1N1) virus deficient in the PB1-F2 protein expression (PR8ΔPB1-F2). These experiments clearly showed that N-terminal region of PB1-F2 protein was responsible for the increase in PB1 protein expression. C-terminal region of PB1-F2 protein had no effect. Thus, we have identified the important function for N-terminal region of PB1-F2 protein.

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Preparation of monoclonal antibodies for the diagnosis of influenza A infection using different immunization protocols

Cited by 41 publications

References 14 publications

Antigenic Profile of Avian H5N1 Viruses in Asia from 2002 to 2007

Antigenic Profile of Avian H5N1 Viruses in Asia from 2002 to 2007

An antibody which binds to the membrane-proximal end of influenza virus haemagglutinin (H3 subtype) inhibits the low-pH-induced conformational change and cell-cell fusion but does not neutralize virus.

N-terminal region of the PB1-F2 protein is responsible for increased expression of influenza A viral protein PB1

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