Recombinant Acinetobacter baumannii Outer membrane protein Omp38 (omp38)

A truncated version of Acinetobacter baumannii outer membrane protein Omp38 lacking the 1-19 amino-acid signal peptide of the C-terminus and carrying a 6xHis-tag at the N-terminus was produced in the yeast. The resulting protein is a full-length of mature Omp38 protein. It contains aa of 20-356 of the Acinetobacter baumannii Omp38 protein. It was purified by SDS-PAGE and reached up to 90% in purity. On the reducing SDS-PAEG gel, this Omp38 protein migrated on the molecular weight band of about 40 kDa. The result is slightly higher than that of the calculated one due to glycosylation. This recombinant Omp38 protein may be used to generate specific antibodies against Omp38 or in the studies of Acinetobacter baumannii infections.

The Acinetobacter baumannii outer membrane protein Omp38, also known as OmpA, is the most abundant surface protein that is responsible for the viral pathogenicity. As a virulence factor, Omp38 is involved in the modulation of adhesion, aggressiveness, and biofilm formation of Acinetobacter baumannii, antibiotic resistance, and the immune reaction of the host. Omp38 has been described as a powerful immunogen to trigger immune responses. It is a potential therapeutic target for the treatment of Acinetobacter baumannii infections.