Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0032285 (pneumonia)
 54,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability to induce protection against a genital challenge was studied in BALB/c female mice with three Chlamydia trachomatis mouse pneumonitis (MoPn) major outer membrane protein (MOMP) preparations as well as an acellular vaccine consisting of the chlamydial outer membrane complex (COMC). The MOMP preparations were extracted with three different types of detergents, sodium dodecyl sulfate (SDS), n-octyl-beta-D-glucopyranoside (OGP), and Zwittergent 3-14 (Z3-14). A positive immunization control consisted of mice inoculated intranasally with 10(4) C. trachomatis MoPn inclusion-forming units (IFU). Mice inoculated with ovalbumin served as a negative control. Furthermore, a sham-immunized, nonchallenged group was included as a fertility control. Two weeks after the last immunization, the mice were challenged in the left ovarian bursa with 10(5) C. trachomatis MoPn IFU. Vaginal swabs were collected for culture, vaginal and serum samples were assayed for chlamydial-specific antibodies, and splenocytes were collected to determine the lymphoproliferative response. At 42 days after the challenge, the mice were mated with proven male breeder mice. Animals that were considered to be pregnant (as determined by weight) were killed, and the embryos were counted. A significant humoral and cell-mediated immune response was observed in all the groups of mice inoculated with chlamydial antigens. Antibodies to variable domain (VD)1 of the MOMP were detected in serum samples from all the immunized groups. However, antibodies to VD3 and VD4 were detected only in the groups immunized with the Z3-14-MOMP and the COMC. Mice immunized with COMC developed significant immunoglobulin A chlamydia-specific antibodies in the vagina, while mice immunized with the detergent-extracted MOMPs had low antibody titers. Following the intrabursal challenge, a significant decrease in the intensity and duration of vaginal shedding was noted in the mice immunized with COMC and a moderate decrease was noted in the group immunized with OGP-MOMP. No protection against the infection was noted in the groups of animals immunized with SDS- and Z3-14-MOMP. Furthermore, of the mice immunized with the COMC preparation, only 25% (4 of 20) shed C. trachomatis, as determined by vaginal culture, while 83% (40 of 48) of the control mice inoculated with ovalbumin were culture positive (P < 0.05). In addition, after mating, the mice inoculated with COMC were found to have fertility rates comparable to those of the control sham-immunized, nonchallenged animals (70% [14 of 20] versus 81% [17 of 21], respectively [P > 0.05]), and there were no significant differences between the average number of embryos per mouse in the two groups (5.1 versus 5.9, respectively [P > 0.05]). In contrast, mice immunized with the purified MOMP preparations were not protected against infertility. In summary, a preparation of the COMC protected mice against infection and infertility, supporting the feasibility of the development of an acellular vaccine against C. trachomatis infections.
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PMID:Immunization with an acellular vaccine consisting of the outer membrane complex of Chlamydia trachomatis induces protection against a genital challenge. 923 98

Pasteurella multocida A:3 is a major cause of bovine pneumonia. A major antigenic heat-modifiable 28kDa outer membrane protein (Omp28) was previously identified. The purpose of this study was to purify and characterize Omp28 immunologically and structurally. Omp28 was extracted from N-lauroylsarcosine-insoluble protein preparations by a combination of detergent fractionation with Zwittergent 3-14 and chromatography. Partial N-terminal amino acid sequence confirmed Omp28 as a member of the OmpA-porin family. However, porin activity could not be demonstrated in a lipid-bilayer assay. Heat modifiability of purified Omp28 was demonstrated, and Omp28 was found in outer membrane fraction of P. multocida. Surface exposure of Omp28 was demonstrated by partial protease digestion of intact bacteria, by binding of anti-Omp28 polyclonal ascites fluid to the bacterial surface, and by partial inhibition of anti-outer membrane antiserum binding by previous incubation of the bacteria with anti-Omp28 serum. CD-1 mice vaccinated with purified Omp28 developed a significant antibody titer (P<0.05) compared to the control treatment group but were not protected from a homologous intraperitoneal bacterial challenge. By contrast, treatment groups vaccinated with P. multocida outer membrane, formalin-killed P. multocida or a commercial vaccine were significantly protected from challenge. In vitro complement-mediated killing of P. multocida was observed in post-vaccination sera of outer membrane, formalin-killed P. multocida, and commercial vaccine-treatment groups, but not with sera from the Omp28-treatment group. In conclusion, although Omp28 is surface exposed and antigenic, it may not be a desirable immunogen for stimulating immunity to P. multocida.
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PMID:Characterization of, and immune responses of mice to, the purified OmpA-equivalent outer membrane protein of Pasteurella multocida serotype A:3 (Omp28). 1205 33