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Immunisation with phage-displayed variable region 2 from meningococcal PorA outer membrane protein induces

T Menéndez1, I De Haz, M Delgado

  • 1Vaccines Division, Center for Genetic Engineering and Biotechnology, Ave.31,entre 158 y 190, Apartado 6162, CP 10600, Havana, Cuba. tamara.menendez@cigb.edu.cu

Immunology Letters
|October 2, 2001
PubMed

Insights

Phage display of a Neisseria meningitidis PorA peptide elicited functional antibodies. A three-glycine linker improved antibody recognition of the native protein and bactericidal activity.

Area of Science:

  • Immunology
  • Microbiology
  • Protein Engineering

Background:

  • PorA is a key outer membrane protein of Neisseria meningitidis.
  • Developing effective vaccines against Neisseria meningitidis requires understanding antibody responses to PorA.
  • Phage display offers a method for presenting peptide antigens.

Purpose of the Study:

  • To evaluate the immunogenicity and functional activity of antibodies against a PorA peptide displayed on phage.
  • To compare the effects of different linkers on antibody responses.

Main Methods:

  • A cyclic disulphide peptide from PorA variable region 2 was displayed on M13 filamentous phage.
  • Peptides were flanked by cysteine or cysteine and a three-glycine linker.
  • Antibodies were generated in mice, and their reactivity and bactericidal activity were assessed.

Main Results:

  • Both phage constructs generated specific antibody responses.
  • Antibodies against the peptide with the three-glycine linker showed better recognition of the native PorA protein.
  • Only antibodies induced by the phage with the linker exhibited bactericidal activity.

Conclusions:

  • Phage display can be used to express conformational peptides for immunization.
  • Linker strategies in phage display can enhance functional antibody responses against bacterial proteins.
  • This approach holds potential for developing novel vaccines against Neisseria meningitidis.

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