Mucosal immunization with caseinolytic protease X elicited cross-protective immunity against pneumococcal infection in mice

Zhong, Wen; Xu, Wenchun; Wang, Hong; Huang, Yuanshuai; Cao, Ju; Gong, Yi; Xu, Xun; Min, Xun; Zhang, Yanqing; Dong, Jing; Yin, Yibing; Zhang, Xuemei

doi:10.1258/ebm.2012.011383

Cited by 7 publications

(3 citation statements)

References 49 publications

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“…Other conserved Sp proteins, such as pneumococcal surface antigen A (PsaA), pneumolysin, pneumolysoid PdT, and histidine triad proteins have been used with potent adjuvants as subunit vaccines that protect mice against pneumonia. 24, 26, 27, 29, 33 Although these studies have not directly tested the role of memory Th17 cells in protection against pneumonia, these findings together with our results support the notion that Th17-inducing conserved Sp protein antigens might be vaccine candidates capable of conferring broad protection by inducing strong memory Th17 responses in the lungs.…”

Section: Resultssupporting

confidence: 70%

Cross-protective mucosal immunity mediated by memory Th17 cells against Streptococcus pneumoniae lung infection

et al. 2017

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Pneumonia caused by Streptococcus pneumoniae (Sp) remains a leading cause of serious illness and death worldwide. Immunization with conjugated pneumococcal vaccine has lowered the colonization rate and consequently invasive diseases by inducing serotype-specific antibodies. However, many of current pneumonia cases result from infection by serotype strains not included in the vaccine. In this study, we asked if cross-protection against lung infection by heterologous strains can be induced and investigated the underlying immune mechanism. We found that immune mice recovered from a prior infection were protected against heterologous Sp strains in the pneumonia challenge model, as evident by accelerated bacterial clearance, reduced pathology and apoptosis of lung epithelial cells. Sp infection in the lung induced strong Th17 responses at the lung mucosal site. Transfer of CD4+ T cells from immune mice provided heterologous protection against pneumonia, and this protection was abrogated by IL-17A blockade. Transfer of memory CD4+ T cells from IL-17A knockout mice failed to provide protection. These results indicate that memory Th17 cells played a key role in providing protection against pneumonia in a serotype independent manner and suggest the feasibility of developing a broadly protective vaccine against bacterial pneumonia by targeting mucosal Th17 T cells.

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Section: Resultssupporting

confidence: 70%

Cross-protective mucosal immunity mediated by memory Th17 cells against Streptococcus pneumoniae lung infection

et al. 2017

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“…For instance, the products of genes of NMB0017, NMB0707, NMB0554, NMB1285, NMB1347 and NMB1372 that are mainly related to enzyme and regulatory cytoplasmic functions have also been identified in previous papers as outer membrane components, exposed on the cell surface or secreted homologues. 69,[78][79][80][81] These results reinforce our previous discussion and the need to encourage a more critical evaluation of the use of subcellular localization predictor software, taking into account that proteins of apparently cytoplasmic origin should not be eliminated from studies without careful consideration and validation.…”

Section: Subcellular Location Predicted By Psortb Software For the Idsupporting

confidence: 81%

A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine againstN. meningitidisserogroup B and C

Masforrol

Gil

García

et al. 2017

Human Vaccines & Immunotherapeutics

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The protein composition of an Outer Membrane Vesicle (OMV) preparation that constitutes the active pharmaceutical ingredient of VA-MENGOC-BC®, an effective vaccine against Neisseria meningitidis serogroups B, and C is presented. This preparation has a high lipid content and five abundant membrane proteins (FetA, PorA, PorB, RmpM, and Opc), constituting approximately 70% of the total protein mass. The protein composition was determined by combining the use of the Hexapeptide Ligand Library and an orthogonal tandem fractionation of tryptic peptides by reverse-phase chromatography at alkaline and acid pH. This approach equalizes the concentration of tryptic peptides derived from low- and high-abundance proteins as well as considerably simplifying the number of peptides analyzed by LC-MS/MS, enhancing the possibility of identifying low-abundance species. Fifty-one percent of the proteins originally annotated as membrane proteins in the genome of the MC58 strain were identified. One hundred and sixty-eight low-abundance cytosolic proteins presumably occluded within OMV were also identified. Four (NadA, NUbp, GNA2091, and fHbp), out of the five antigens constituting the Bexsero® vaccine, were detected in this OMV preparation. In particular, fHbp is also the active principle of the Trumenba® vaccine developed by Pfizer. The HpuA and HpuB gene products (not annotated in the MC58 genome) were identified in the CU385 strain, a clinical isolate that is used to produce this OMV. Considering the proteins identified here and previous work done by our group, the protein catalogue of this OMV preparation was extended to 266 different protein species.

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“…coli [ 60 ]. ClpX was shown to have potential use in a vaccine to protect against the nasopharyngeal colonization of Streptococcus pneumoniae in mice [ 61 ]. OmpA is a major immunoreactive E .…”

Section: Discussionmentioning

confidence: 99%

Protective Enterotoxigenic Escherichia coli Antigens in a Murine Intranasal Challenge Model

et al. 2015

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Enterotoxigenic Escherichia coli (ETEC) is an endemic health threat in underdeveloped nations. Despite the significant effort extended to vaccine trials using ETEC colonization factors, these approaches have generally not been especially effective in mediating cross-protective immunity. We used quantitative proteomics to identify 24 proteins that differed in abundance in membrane protein preparations derived from wild-type vs. a type II secretion system mutant of ETEC. We expressed and purified a subset of these proteins and identified nine antigens that generated significant immune responses in mice. Sera from mice immunized with either the MltA-interacting protein MipA, the periplasmic chaperone seventeen kilodalton protein, Skp, or a long-chain fatty acid outer membrane transporter, ETEC_2479, reduced the adherence of multiple ETEC strains differing in colonization factor expression to human intestinal epithelial cells. In intranasal challenge assays of mice, immunization with ETEC_2479 protected 88% of mice from an otherwise lethal challenge with ETEC H10407. Immunization with either Skp or MipA provided an intermediate degree of protection, 68 and 64%, respectively. Protection was significantly correlated with the induction of a secretory immunoglobulin A response. This study has identified several proteins that are conserved among heterologous ETEC strains and may thus potentially improve cross-protective efficacy if incorporated into future vaccine designs.

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Mucosal immunization with caseinolytic protease X elicited cross-protective immunity against pneumococcal infection in mice

Cited by 7 publications

References 49 publications

Cross-protective mucosal immunity mediated by memory Th17 cells against Streptococcus pneumoniae lung infection

Cross-protective mucosal immunity mediated by memory Th17 cells against Streptococcus pneumoniae lung infection

A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine againstN. meningitidisserogroup B and C

Protective Enterotoxigenic Escherichia coli Antigens in a Murine Intranasal Challenge Model

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