Structural Assessment of Chlamydia trachomatis Major Outer Membrane Protein (MOMP)-Derived Vaccine Antigens and Immunological Profiling in Mice with Different Genetic Backgrounds

• Published in: Vaccines (Basel) Vol. 12; no. 7; p. 789
• Main Authors: Roe, Shea K, Zhu, Tianmou, Slepenkin, Anatoli, Berges, Aym, Fairman, Jeff, de la Maza, Luis M, Massari, Paola
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01-07-2024
• Subjects: Adjuvants; Antibiotics; Antibodies; Antigens; B-cell epitopes; Bacterial vaccines; CD4 antigen; Cellular manufacture; Cellular structure; Chlamydia; Chlamydia trachomatis; Chromatography; Cloning; Complications; Dosage and administration; Evaluation; Identification and classification; Immunogenicity; Immunoglobulin G; Immunology; Infections; Lymphocytes; Lymphocytes T; Major outer membrane protein; Membrane proteins; Membranes; MOMP; Neutralizing; Prevention; Proteins; Reproductive system; Respiratory tract infection; Risk factors; Sensors; Sexually transmitted diseases; Splenocytes; STD; Structural analysis; Structure; Testing; vaccine; Vaccines; γ-Interferon; United States; United States > US; B-cell epitopes; MOMP; vaccine; Chlamydia trachomatis; antibodies
• ISSN: 2076-393X; 2076-393X
• DOI: 10.3390/vaccines12070789

(
) is the most common cause of bacterial sexually transmitted infections (STIs) worldwide.
infections are often asymptomatic in women, leading to severe reproductive tract sequelae. Development of a vaccine against
is crucial. The
major outer membrane protein (MOMP) is a prime vaccine antigen candidate, and it can elicit both neutralizing antibodies and protective CD4+ T cell responses. We have previously designed chimeric antigens composed of immunogenic variable regions (VDs) and conserved regions (CDs) of MOMP from
(
) expressed into a carrier protein (PorB), and we have shown that these were protective in a mouse model of
respiratory infection. Here, we generated corresponding constructs based on MOMP from
serovar F. Preliminary structure analysis of the three antigens, PorB/VD1-3, PorB/VD1-4 and PorB/VD1-2-4, showed that they retained structure features consistent with those of PorB. The antigens induced robust humoral and cellular responses in mice with different genetic backgrounds. The antibodies were cross-reactive against
but only anti-PorB/VD1-4 and anti-PorB/VD1-2-4 IgG antibodies were neutralizing, likely due to the antigen specificity. The cellular responses included proliferation in vitro and production of IFN-γ by splenocytes following
re-stimulation. Our results support further investigation of the PorB/VD antigens as potential protective candidates for a
subunit vaccine.