Protection against Salmonella typhi infection in mice after immunization with outer membrane proteins isolated from Salmonella typhi 9,12,d, Vi

Isibasí, Armando; Ortiz, Vianey; Vargas, Mauricio Salcedo; Paniagua, Jorge; Gonzalez, Christian; Moreno, José María Villagrán; Kumate, J

doi:10.1128/iai.56.11.2953-2959.1988

Cited by 110 publications

(34 citation statements)

References 36 publications

(30 reference statements)

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“…Porins induce effective humoral immune response as reflected in the increased antibodies as compared to the controls. It has been previously shown that the passive transfer of anti-porin antibodies could provide protection (17,33). The Vi-CPS also induces antibody responses primarily of the IgM isotype, as observed in the present study and supported by earlier findings (1,23).…”

Section: Discussionsupporting

confidence: 92%

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Protective Efficacy and Immunogenicity of Vi‐Porin Conjugate against Salmonella typhi

Singh

Ganguly

Kumar

et al. 1999

Microbiology and Immunology

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A conjugate vaccine against Salmonella typhi was prepared by covalently binding capsular polysaccharide (Vi) with porin, both isolated from S. typhi. First, Vi and porins were extracted. The Vi was purified from S. typhi Ty2. The purified Vi conformed to the requirements of the World Health Organization. Porins were purified from S. typhi 0901. The Vi was bound to the porins by a heterobifunctional cross‐linking reagent, N‐succinimidyl‐3‐(2‐pyridyl dithio)‐propionate (SPDP). After preparing the Vi‐porin conjugate, its protective ability and immunogenicity were studied in mice following systemic immunization. The results showed that the conjugate is 6.5‐fold more protective than Vi alone against S. typhi. The mice immunized with conjugate elicited higher anti‐Vi antibody (IgG) levels (P<0.01) than the mice immunized with Vi alone. Anti‐porin antibodies were also induced by the conjugate. To study the mucosal immune responses, secretory IgA (sIgA) in the intestinal fluid was measured. Conjugate‐immunized mice showed the induction of sIgA as compared to Vi alone. The results showed that when Vi is bound to porins, both isolated from same organism, the resultant conjugate induced both systemic and mucosal immune responses and provided better protection against S. typhi than Vi alone.

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Section: Discussionsupporting

confidence: 92%

“…Recently, attention is focussed on the possible use of outer membrane protein, particularly porins, as subunit vaccines against S. typhi, S. typhimurium, Escherichia coli, Pseudomonas aeruginosa, etc. (17,19,27,34). Results showed that they are good immunogens.…”

mentioning

confidence: 99%

Protective Efficacy and Immunogenicity of Vi‐Porin Conjugate against Salmonella typhi

Singh

Ganguly

Kumar

et al. 1999

Microbiology and Immunology

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“…The S. fyp/7/strains (serotypes 9,12, d and Vi) were the following: IMSS-I, isolated from a patient with TF, generously donated by Dr Jesus Kumate and collaborators (Instituto Mexicano del Seguro Social, Mexico DF) (Isibasi et al, 1988); Ty2, obtained from the American Type Culture Collection (ATCC No. 19430): and eight clinical isolates of the MK series, isolated from TF patients with different clinical symptoms, generously made available by Dr Guillermo Ruiz-Palacios and collaborators (Instituto Nacional de la Nutricion 'Salvador Zubiran', Mexico DF).…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

Expression of Salmonella typhi and Escherichia coli OmpC is influenced differently by medium osmolarity; dependence on Escherichia coli OmpR

Puente

Verdugo-Rodríguez

Calva

1991

Molecular Microbiology

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OmpC, a major outer-membrane protein, is highly expressed when Salmonella typhi is grown in nutrient broth (NB) of either low (NB + 0% sucrose) or high (NB + 20% sucrose) osmolarity. This contrasts with the expression of Escherichia coli OmpC, which is inhibited in low osmolarity and enhanced in high osmolarity, as has been described previously (van Alphen and Lugtenberg, 1977; Verhoef et al., 1979; Kawaji et al., 1979). Nevertheless, expression of S. typhi OmpC is dependent on the E. coli OmpR transcriptional activator. These findings suggest differences between the mechanisms of osmoregulation of gene expression in both bacteria, although common effectors appear to be shared.

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“…The S. Typhi STYompFC mutant strain (formerly VALE39 7 ), which was deficient for both OmpF and OmpC (ΔompF Km R and ΔompC Cm R ), was generated using site-directed mutagenesis 22 of the IMSS-1 Mexican wild-type reference strain. 23,24 This mutant strain was then transformed with one of the plasmids pF2 (expressing OmpS1 15 ) or pFM97S2 (expressing OmpS2 16 ).…”

Section: Bacterial Strainsmentioning

confidence: 99%

Salmonella Typhi OmpS1 and OmpS2 porins are potent protective immunogens with adjuvant properties

et al. 2013

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Summary Salmonella enterica serovar Typhi (S. Typhi) is the causal agent of typhoid fever, a disease that primarily affects developing countries. Various antigens from this bacterium have been reported to be targets of the immune response. Recently, the S. Typhi genome has been shown to encode two porins – OmpS1 and OmpS2 – which are expressed at low levels under in vitro culture conditions. In this study, we demonstrate that immunizing mice with either OmpS1 or OmpS2 induced production of specific, long‐term antibody titres and conferred protection against S. Typhi challenge; in particular, OmpS1 was more immunogenic and conferred greater protective effects than OmpS2. We also found that OmpS1 is a Toll‐like receptor 4 (TLR4) agonist, whereas OmpS2 is a TLR2 and TLR4 agonist. Both porins induced the production of tumour necrosis factor and interleukin‐6, and OmpS2 was also able to induce interleukin‐10 production. Furthermore, OmpS1 induced the over‐expression of MHC II molecules in dendritic cells and OmpS2 induced the over‐expression of CD40 molecules in macrophages and dendritic cells. Co‐immunization of OmpS1 or OmpS2 with ovalbumin (OVA) increased anti‐OVA antibody titres, the duration and isotype diversity of the OVA‐specific antibody response, and the proliferation of T lymphocytes. These porins also had adjuvant effects on the antibody response when co‐immunized with either the Vi capsular antigen from S. Typhi or inactivated 2009 pandemic influenza A(H1N1) virus [A(H1N1)pdm09]. Taken together, the data indicate that OmpS1 and OmpS2, despite being expressed at low levels under in vitro culture conditions, are potent protective immunogens with intrinsic adjuvant properties.

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Protection against Salmonella typhi infection in mice after immunization with outer membrane proteins isolated from Salmonella typhi 9,12,d, Vi

Abstract: The current studies were undertaken to assess the ability of the outer membrane proteins (OMPs) of Salmonella typhi to induce protection against challenge with the bacteria in mucin. OMPs were isolated as 2953

Cited by 110 publications

References 36 publications

Protective Efficacy and Immunogenicity of Vi‐Porin Conjugate against Salmonella typhi

Protective Efficacy and Immunogenicity of Vi‐Porin Conjugate against Salmonella typhi

Expression of Salmonella typhi and Escherichia coli OmpC is influenced differently by medium osmolarity; dependence on Escherichia coli OmpR

Salmonella Typhi OmpS1 and OmpS2 porins are potent protective immunogens with adjuvant properties

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