Mapping the Intersubunit Region of Influenza Virus Hemagglutinin: Comparative CD and FTIR Spectroscopic Studies on Multiple Antigenic Peptides

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Abstract

An A/PR/8/34 (IHN1) influenza virus hemagglutinin (HA)-specific monoclonal antibody (Z38) was found to react with the solid phase adsorbed influenza virus expressing uncleaved (HA0) molecules but not to bind to virus particles bearing enzymatically cleaved hemagglutinin. Synthetic peptides corresponding to the uncleaved HA0 317-341 intersubunit region of subtypes H1-H3 (IP1-IP3) or comprising either the C-terminal 317-329 amino acids of HA1 (CPI) or the N-terminal 330-341 of HA2 (fusion peptide, FP) subunits of cleaved HA were used to characterize the the specificity of 238 mAb, Circular dichroism and Fourier-transform infrared spectroscopy showed that, compared to IP2 and IP3 comprising the H2 and H3 subtype fragments of the intact intersubunit region, IP1 has relatively low helicity but a tendency to adopt β-turns in trifluoroethanol. The immunological and conformational properties of multiple antigenic peptides (MAPs) containing four copies of CPI were also studied, Based on the appearance of an infrared component band at 1637 cm-1 (β-turn band), the CP1 arms of MAPs also contain repeats of β-turns. However, it is only the MAP1-FP construct comprising also the fusion peptide, which binds Z38 mAb as strongly as IP1 does. This puts emphasis on the role of the fusion region in modifying conformation and consequently the ability of peptides to elicit an antibody response. The results obtained for peptide conformation also suggests a β-turn(s)/β-sheet/β-turn/β-sheet conformationaI motif in the recognition by the hemagglutinin subtype-specific Z38 monoclonal antibody or by peptide-induced polyclonal antibodies.

Original languageEnglish
Pages (from-to)112-118
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume322
Issue number1
DOIs
Publication statusPublished - Sep 10 1995

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Hemagglutinins
Fourier Transform Infrared Spectroscopy
Orthomyxoviridae
Viruses
Peptides
Fusion reactions
Conformations
Bearings (structural)
Monoclonal Antibodies
Trifluoroethanol
Antibodies
Circular Dichroism
Virion
Antibody Formation
Infrared radiation
Amino Acids
Molecules

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

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title = "Mapping the Intersubunit Region of Influenza Virus Hemagglutinin: Comparative CD and FTIR Spectroscopic Studies on Multiple Antigenic Peptides",
abstract = "An A/PR/8/34 (IHN1) influenza virus hemagglutinin (HA)-specific monoclonal antibody (Z38) was found to react with the solid phase adsorbed influenza virus expressing uncleaved (HA0) molecules but not to bind to virus particles bearing enzymatically cleaved hemagglutinin. Synthetic peptides corresponding to the uncleaved HA0 317-341 intersubunit region of subtypes H1-H3 (IP1-IP3) or comprising either the C-terminal 317-329 amino acids of HA1 (CPI) or the N-terminal 330-341 of HA2 (fusion peptide, FP) subunits of cleaved HA were used to characterize the the specificity of 238 mAb, Circular dichroism and Fourier-transform infrared spectroscopy showed that, compared to IP2 and IP3 comprising the H2 and H3 subtype fragments of the intact intersubunit region, IP1 has relatively low helicity but a tendency to adopt β-turns in trifluoroethanol. The immunological and conformational properties of multiple antigenic peptides (MAPs) containing four copies of CPI were also studied, Based on the appearance of an infrared component band at 1637 cm-1 (β-turn band), the CP1 arms of MAPs also contain repeats of β-turns. However, it is only the MAP1-FP construct comprising also the fusion peptide, which binds Z38 mAb as strongly as IP1 does. This puts emphasis on the role of the fusion region in modifying conformation and consequently the ability of peptides to elicit an antibody response. The results obtained for peptide conformation also suggests a β-turn(s)/β-sheet/β-turn/β-sheet conformationaI motif in the recognition by the hemagglutinin subtype-specific Z38 monoclonal antibody or by peptide-induced polyclonal antibodies.",
author = "Zs. Majer and S. Holly and G. T{\'o}th and G. Varadi and Z. Nagy and A. Horv{\'a}th and E. Rajnavolgyi and I. Laczk{\'o} and M. Holl{\'o}si",
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T1 - Mapping the Intersubunit Region of Influenza Virus Hemagglutinin

T2 - Comparative CD and FTIR Spectroscopic Studies on Multiple Antigenic Peptides

AU - Majer, Zs.

AU - Holly, S.

AU - Tóth, G.

AU - Varadi, G.

AU - Nagy, Z.

AU - Horváth, A.

AU - Rajnavolgyi, E.

AU - Laczkó, I.

AU - Hollósi, M.

PY - 1995/9/10

Y1 - 1995/9/10

N2 - An A/PR/8/34 (IHN1) influenza virus hemagglutinin (HA)-specific monoclonal antibody (Z38) was found to react with the solid phase adsorbed influenza virus expressing uncleaved (HA0) molecules but not to bind to virus particles bearing enzymatically cleaved hemagglutinin. Synthetic peptides corresponding to the uncleaved HA0 317-341 intersubunit region of subtypes H1-H3 (IP1-IP3) or comprising either the C-terminal 317-329 amino acids of HA1 (CPI) or the N-terminal 330-341 of HA2 (fusion peptide, FP) subunits of cleaved HA were used to characterize the the specificity of 238 mAb, Circular dichroism and Fourier-transform infrared spectroscopy showed that, compared to IP2 and IP3 comprising the H2 and H3 subtype fragments of the intact intersubunit region, IP1 has relatively low helicity but a tendency to adopt β-turns in trifluoroethanol. The immunological and conformational properties of multiple antigenic peptides (MAPs) containing four copies of CPI were also studied, Based on the appearance of an infrared component band at 1637 cm-1 (β-turn band), the CP1 arms of MAPs also contain repeats of β-turns. However, it is only the MAP1-FP construct comprising also the fusion peptide, which binds Z38 mAb as strongly as IP1 does. This puts emphasis on the role of the fusion region in modifying conformation and consequently the ability of peptides to elicit an antibody response. The results obtained for peptide conformation also suggests a β-turn(s)/β-sheet/β-turn/β-sheet conformationaI motif in the recognition by the hemagglutinin subtype-specific Z38 monoclonal antibody or by peptide-induced polyclonal antibodies.

AB - An A/PR/8/34 (IHN1) influenza virus hemagglutinin (HA)-specific monoclonal antibody (Z38) was found to react with the solid phase adsorbed influenza virus expressing uncleaved (HA0) molecules but not to bind to virus particles bearing enzymatically cleaved hemagglutinin. Synthetic peptides corresponding to the uncleaved HA0 317-341 intersubunit region of subtypes H1-H3 (IP1-IP3) or comprising either the C-terminal 317-329 amino acids of HA1 (CPI) or the N-terminal 330-341 of HA2 (fusion peptide, FP) subunits of cleaved HA were used to characterize the the specificity of 238 mAb, Circular dichroism and Fourier-transform infrared spectroscopy showed that, compared to IP2 and IP3 comprising the H2 and H3 subtype fragments of the intact intersubunit region, IP1 has relatively low helicity but a tendency to adopt β-turns in trifluoroethanol. The immunological and conformational properties of multiple antigenic peptides (MAPs) containing four copies of CPI were also studied, Based on the appearance of an infrared component band at 1637 cm-1 (β-turn band), the CP1 arms of MAPs also contain repeats of β-turns. However, it is only the MAP1-FP construct comprising also the fusion peptide, which binds Z38 mAb as strongly as IP1 does. This puts emphasis on the role of the fusion region in modifying conformation and consequently the ability of peptides to elicit an antibody response. The results obtained for peptide conformation also suggests a β-turn(s)/β-sheet/β-turn/β-sheet conformationaI motif in the recognition by the hemagglutinin subtype-specific Z38 monoclonal antibody or by peptide-induced polyclonal antibodies.

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