Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis

Dai Fang Liu, Xiaoling Xie, Maria G. Mastri, Maria Fortuna-Nevin, Christopher Colocillo, Leah Fletcher, Deborah A. Dilts, John C. McMichael, Steven M. Baker

Research output: Contribution to journalArticle

Original languageEnglish (US)
Pages (from-to)343-350
Number of pages8
JournalFEMS Immunology and Medical Microbiology
Volume47
Issue number3
DOIs
StatePublished - Aug 1 2006
Externally publishedYes

Fingerprint

Moraxella (Branhamella) catarrhalis
Epitopes
Membrane Proteins
Serum
Vaccines
Recombinant Proteins
Moraxellaceae Infections
Peptides
Amino Acid Sequence
Western Blotting
Enzyme-Linked Immunosorbent Assay
Monoclonal Antibodies
Antigens
Infection
Genes
Proteins

Keywords

  • CopB
  • Moraxella catarrhalis
  • Surface epitope sequence variation
  • Vaccine

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)
  • Infectious Diseases

Cite this

Liu, D. F., Xie, X., Mastri, M. G., Fortuna-Nevin, M., Colocillo, C., Fletcher, L., ... Baker, S. M. (2006). Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis. FEMS Immunology and Medical Microbiology, 47(3), 343-350. https://doi.org/10.1111/j.1574-695X.2006.00093.x

Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis. / Liu, Dai Fang; Xie, Xiaoling; Mastri, Maria G.; Fortuna-Nevin, Maria; Colocillo, Christopher; Fletcher, Leah; Dilts, Deborah A.; McMichael, John C.; Baker, Steven M.

In: FEMS Immunology and Medical Microbiology, Vol. 47, No. 3, 01.08.2006, p. 343-350.

Research output: Contribution to journalArticle

Liu, DF, Xie, X, Mastri, MG, Fortuna-Nevin, M, Colocillo, C, Fletcher, L, Dilts, DA, McMichael, JC & Baker, SM 2006, 'Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis', FEMS Immunology and Medical Microbiology, vol. 47, no. 3, pp. 343-350. https://doi.org/10.1111/j.1574-695X.2006.00093.x
Liu, Dai Fang ; Xie, Xiaoling ; Mastri, Maria G. ; Fortuna-Nevin, Maria ; Colocillo, Christopher ; Fletcher, Leah ; Dilts, Deborah A. ; McMichael, John C. ; Baker, Steven M. / Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis. In: FEMS Immunology and Medical Microbiology. 2006 ; Vol. 47, No. 3. pp. 343-350.
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title = "Polymorphism of the major surface epitope of the CopB outer membrane protein of Moraxella catarrhalis",
abstract = "The CopB outer membrane protein has been considered a vaccine candidate for the prevention of infections due to Moraxella catarrhalis. Monoclonal antibody 10F3 recognizes whole cells of about 70{\%} of clinical isolates, suggesting that this epitope is reasonably conserved. To determine whether CopB has other surface epitopes, we analyzed M. catarrhalis isolates using polyclonal sera against recombinant CopB proteins from a 10F3 positive isolate and a 10F3 negative isolate, and polyclonal sera against synthetic peptides that contained the sequence corresponding to the 10F3 epitope region of three different isolates. Extensive cross-reactivity was observed with the anti-CopB sera towards purified recombinant CopB proteins in Western blot and antigen ELISA, implying that antigenic regions common to both proteins were present. However, anti-CopB sera resembled anti-CopB peptide sera in exhibiting similar binding specificity to whole cells, segregating M. catarrhalis isolates into four CopB groups. We subsequently cloned and sequenced the copB genes from representative isolates. The deduced CopB amino acid sequences and the degree of sequence identity also demonstrated the existence of the same four CopB groups. Each of the four groups had a unique sequence in the 10F3 epitope region and a fifth group had the epitope deleted. The polymorphism of the major surface epitope prompts further consideration regarding the utility of CopB as a vaccine component as well as the design of an efficacious CopB-based vaccine to achieve broad protection against Moraxella infection.",
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N2 - The CopB outer membrane protein has been considered a vaccine candidate for the prevention of infections due to Moraxella catarrhalis. Monoclonal antibody 10F3 recognizes whole cells of about 70% of clinical isolates, suggesting that this epitope is reasonably conserved. To determine whether CopB has other surface epitopes, we analyzed M. catarrhalis isolates using polyclonal sera against recombinant CopB proteins from a 10F3 positive isolate and a 10F3 negative isolate, and polyclonal sera against synthetic peptides that contained the sequence corresponding to the 10F3 epitope region of three different isolates. Extensive cross-reactivity was observed with the anti-CopB sera towards purified recombinant CopB proteins in Western blot and antigen ELISA, implying that antigenic regions common to both proteins were present. However, anti-CopB sera resembled anti-CopB peptide sera in exhibiting similar binding specificity to whole cells, segregating M. catarrhalis isolates into four CopB groups. We subsequently cloned and sequenced the copB genes from representative isolates. The deduced CopB amino acid sequences and the degree of sequence identity also demonstrated the existence of the same four CopB groups. Each of the four groups had a unique sequence in the 10F3 epitope region and a fifth group had the epitope deleted. The polymorphism of the major surface epitope prompts further consideration regarding the utility of CopB as a vaccine component as well as the design of an efficacious CopB-based vaccine to achieve broad protection against Moraxella infection.

AB - The CopB outer membrane protein has been considered a vaccine candidate for the prevention of infections due to Moraxella catarrhalis. Monoclonal antibody 10F3 recognizes whole cells of about 70% of clinical isolates, suggesting that this epitope is reasonably conserved. To determine whether CopB has other surface epitopes, we analyzed M. catarrhalis isolates using polyclonal sera against recombinant CopB proteins from a 10F3 positive isolate and a 10F3 negative isolate, and polyclonal sera against synthetic peptides that contained the sequence corresponding to the 10F3 epitope region of three different isolates. Extensive cross-reactivity was observed with the anti-CopB sera towards purified recombinant CopB proteins in Western blot and antigen ELISA, implying that antigenic regions common to both proteins were present. However, anti-CopB sera resembled anti-CopB peptide sera in exhibiting similar binding specificity to whole cells, segregating M. catarrhalis isolates into four CopB groups. We subsequently cloned and sequenced the copB genes from representative isolates. The deduced CopB amino acid sequences and the degree of sequence identity also demonstrated the existence of the same four CopB groups. Each of the four groups had a unique sequence in the 10F3 epitope region and a fifth group had the epitope deleted. The polymorphism of the major surface epitope prompts further consideration regarding the utility of CopB as a vaccine component as well as the design of an efficacious CopB-based vaccine to achieve broad protection against Moraxella infection.

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