3D structure analysis of PorB Outer Membrane Protein in Neisseria meningitides

Fahime sadat Mousavi zade¹ Fateme Sefid² Mohadese Akhondi aghda³ Sara Sabet⁴ Afsane Bastani allah abadi⁵ Sadaf Jelvani⁶

1) Undergraduate Student of Cell and Molecular Biology of Science and Arts University, Yazd, Iran
2) Graduate Student of Cell and Molecular Biology of Shahed University, Tehran, Iran
3) Undergraduate Student of Cell and Molecular Biology of Science and Arts University, Yazd, Iran
4) Undergraduate Student of Cell and Molecular Biology of Science and Arts University, Yazd, Iran
5) Undergraduate Student of Cell and Molecular Biology of Science and Arts University, Yazd, Iran
6) Undergraduate Student of Cell and Molecular Biology of Science and Arts University, Yazd, Iran

Publication : International Conference on Engineering and Applied Science(iceasconf.com)
Abstract :
The development of an effective vaccine against life-threatening episodes of meningitis and septicaemia, caused by serogroup B strains of Neisseria meningitidis, is a continuing healthcare priority. The meningococcal porin proteins induce an antibody response during infection, which correlates with the development of bactericidal and opsonic activity. PorA protein has been identified as making a major contribution to the development of bactericidal activity after immunization of volunteers with the experimental OMV vaccine. However, it has been suggested that the reduced size of the surface-exposed loops of PorB, particularly PorB3, compared with PorA make it less accessible to antibodies and hence less susceptible to immunological attack after immunization with OMV. Nevertheless, some monoclonal antibodies directed against PorB3 demonstrate bactericidal activity , suggesting that it remains a potential vaccine candidate. In order to study the vaccine potential of individual outer membrane proteins, we analyze the PorB structure to identified functional residues which involved in ligand binding site.
Keywords : PorB in silico 3D structure ligand binding site