Abstract
Chlamydia trachomatis (C. trachomatis) is the leading cause of preventable blindness worldwide and the most prevalent cause of bacterial sexually transmitted diseases. At present, there is no available vaccine, and recurrences after antibiotics treatment are substantial problems. Major outer membrane protein (MOMP) accounts for 60% of the outer mass of C. trachomatis, functioning as trimeric porin, and it is highly antigenic. Therefore, MOMP is the most promising candidate for vaccine developing and target therapy of Chlamydia. Affibody, a new class of affinity ligands derived from the Z-domain in the binding region of Staphylococcus aureus protein A, has been the focus of researchers as a viable alternative to antibodies. In this study, the MOMP-targeted affibody molecule (ZMOMP:461) was screened by phage-displayed peptide library. Further, the affinity and specificity were characterized by surface plasmon resonance (SPR) and Western blot. Immunofluorescence assay (IFA) indicated that the MOMP-binding affibody could recognize native MOMP in HeLa229 cells infected C. trachomatis. Immunoprecipitation assay confirmed further that ZMOMP:461 molecule specifically recognizes the epitope on relaxed trimer MOMP. Our findings provide strong evidence that affibody molecule (ZMOMP:461) serves as substitute for MOMP antibody for biological applications and has a great potential for delivering drugs for target therapy.Key points• We screened a novel affibody molecule ZMOMP:461 targeting Chlamydia trachomatis MOMP.• ZMOMP:461 recognizes the recombinant and native MOMP with high affinity and specificity.• ZMOMP:461 could be internalized into live target cells.
Highlights
Chlamydia trachomatis (C. trachomatis), an obligate intracellular bacterium, is the most common sexually transmitted bacterial pathogen worldwide (Centers for CDC 2015; Workowski and Bolan 2015)
The above data indicated that major outer membrane protein (MOMP) antiserum prepared in-house could recognize the compact trimer and monomer MOMP derived from infected HeLa229 cells and was used for subsequent investigations
Increasing concentrations of ZMOMP:461 led to dose-dependent increase of the response intensity, while ZWT could not be detected in any effective interaction with MOMP fusion protein
Summary
Chlamydia trachomatis (C. trachomatis), an obligate intracellular bacterium, is the most common sexually transmitted bacterial pathogen worldwide (Centers for CDC 2015; Workowski and Bolan 2015). The majority of genital Chlamydial infection may result in severe complications such. Previous studies have shown that the cysteine-rich major outer membrane protein (MOMP) may function as a Chlamydial adhesin by promoting nonspecific interactions with host cells (Su et al 1990; Mehlitz and Rudel 2013). MOMP makes up 60% of the total outer membrane protein and is thought to play a role in maintaining structural integrity of the organism (Caldwell et al 1981; Caldwell and Judd 1982) by forming a trimeric structure (Sun et al 2007). MOMP is regarded as a promising candidate for development of vaccine and novel therapeutics to treat Chlamydia infection
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