Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella

Xiao Wang, Da Teng, Qingfeng Guan, Ruoyu Mao, Ya Hao, Xiumin Wang, Junhu Yao, Jianhua Wang

Diarrhea caused by pathogenic Escherichia coli (E. coli) is one of the most serious infectious diseases in humans and animals. Due to antibiotics resistance and the lack of efficient vaccine, more attention should be paid to find potential versatile vaccine candidates to prevent diseases. In this study, the sequence homology analysis indicated that OmpF from E. coli CVCC 1515 shares a high identity (90-100%) with about half of the E. coli (46.7%) and Shigella (52.8%) strains. Then the recombinant OmpF was supposed to be developed as a versatile vaccine to prevent E. coli infection. OmpF was expressed in E. coli BL21 (DE3) using the auto-induction method. The recombinant OmpF (rOmpF) protein had an average molecular weight of 40 kDa with the purity of 90%. Immunological analysis indicated that the titers of anti-rOmpF sera against rOmpF and whole cells were 1:240,000 and 1:27,000, respectively. The opsonophagocytosis result showed that 72.21 ± 11.39 and 11.04 ± 3.90% of bacteria were killed in the rOmpF immunization and control groups, respectively. The survival ratio of mice immunized with rOmpF ranged between 40 and 60% as observed within 36 h after challenge, indicating mice were partially protected from E. coli CVCC 1515 infection. The expressed rOmpF protein induced an effective immune response, but only provide a weak protection against pathogenic E. coli CVCC 1515 and a small reduction in E. coli CICC 21530 (O157:H7) excretion in a mouse infection model. Native forms of the OmpF antigen may be studied for immunogenicity and potential protective efficacy.