scholarly journals Priming with Chlamydia trachomatis Major Outer Membrane Protein (MOMP) DNA followed by MOMP ISCOM Boosting Enhances Protection and Is Associated with Increased Immunoglobulin A and Th1 Cellular Immune Responses

2000 ◽  
Vol 68 (6) ◽  
pp. 3074-3078 ◽  
Author(s):  
Zhang Dong-Ji ◽  
Xi Yang ◽  
Caixia Shen ◽  
Hong Lu ◽  
Andrew Murdin ◽  
...  

ABSTRACT We previously reported that DNA vaccination was able to elicit cellular immune responses and partial protection againstChlamydia trachomatis infection. However, DNA immunization alone did not generate immune responses or protection as great as that induced by using live organisms. In this study, we evaluated the immunologic effects of a combinational vaccination approach usingC. trachomatis mouse pneumonitis (MoPn) major outer membrane protein (MOMP) DNA priming followed by boosting with immune-stimulating complexes (ISCOM) of MOMP protein (MOMP ISCOM) for protection of BALB/c mice against MoPn lung infection. Substantially better protection to challenge infection was observed in mice given combinational vaccination compared with mice given MOMP ISCOM immunization alone, and the protection approximated that induced by live organisms. Enhanced protection was correlated with stronger delayed-type hypersensitivity, higher levels of gamma interferon production, and increased immunoglobulin A antibody responses in lung homogenates. The results indicate that DNA priming followed by ISCOM protein boosting may be useful in designing a fully protective chlamydial vaccine.

2008 ◽  
Vol 8 (4) ◽  
pp. 207-215 ◽  
Author(s):  
Pragya Srivastava ◽  
Rishein Gupta ◽  
Hem Chandra Jha ◽  
Rajneesh Jha ◽  
Apurb Rashmi Bhengraj ◽  
...  

2019 ◽  
Vol 221 (2) ◽  
pp. 191-200 ◽  
Author(s):  
Delia F Tifrea ◽  
Sukumar Pal ◽  
Luis M de la Maza

Abstract Background Chlamydia trachomatis is the most common sexually transmitted bacterial pathogen worldwide. Here, we determined the ability of a C. trachomatis recombinant major outer membrane protein (rMOMP) vaccine to elicit cross-serogroup protection. Methods Female C3H/HeN mice were vaccinated by mucosal and systemic routes with C. trachomatis serovar D (UW-3/Cx) rMOMP and challenged in the ovarian bursa with serovars D (UW-3/Cx), D (UCI-96/Cx), E (IOL-43), or F (N.I.1). CpG-1826 and Montanide ISA 720 were used as adjuvants. Results Immune responses following vaccination were more robust against the most closely related serovars. Following a genital challenge (as determined by number of mice with positive vaginal cultures, number of positive cultures, number of inclusion forming units recovered, and number of days with positive cultures) mice challenged with C. trachomatis serovars of the same complex were protected but not those challenged with serovar F (N.I.1) from a different subcomplex. Females were caged with male mice. Based on fertility rates, number of embryos, and hydrosalpinx formation, vaccinated mice were protected against challenges with serovars D (UW-3/Cx), D (UCI-96/Cx), and E (IOL-43) but not F (N.I.1). Conclusions This is the first subunit vaccine shown to protect mice against infection, pathology, and infertility caused by different C. trachomatis serovars.


Immunobiology ◽  
2011 ◽  
Vol 216 (1-2) ◽  
pp. 152-163 ◽  
Author(s):  
Alexandra Bermudez-Fajardo ◽  
Anne-Katrien Stark ◽  
Rehab El-Kadri ◽  
Manuel L. Penichet ◽  
Katharina Hölzle ◽  
...  

2001 ◽  
Vol 183 (8) ◽  
pp. 2686-2690 ◽  
Author(s):  
Regina J. Tanzer ◽  
Thomas P. Hatch

ABSTRACT We used a photoactivatable, lipophilic reagent, 3′-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, to label proteins in the outer membrane of elementary bodies ofChlamydia trachomatis LGV serovar L2 and mass spectrometry to identify the labeled proteins. The identified proteins were polymorphic outer membrane proteins E, G, and H, which were made late in the developmental cycle, the major outer membrane protein, and a mixture of 46-kDa proteins consisting of the open reading frame 623 protein and possibly a modified form of the major outer membrane protein.


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