Expression and characterization of cholera toxin B—pneumococcal surface adhesin A fusion protein in Escherichia coli: ability of CTB-PsaA to induce humoral immune response in mice

Arêas, Ana Paula Mattos; Oliveira, Maria Leonor S.; Miyaji, Eliane N.; Leite, Luciana C. C.; Aires, Karina Araújo; Dias, Waldely O.; Ho, Paulo Lee

doi:10.1016/j.bbrc.2004.06.118

Cited by 58 publications

(43 citation statements)

References 18 publications

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“…1, only animals immunized with the fusion protein were able to produce high titers of serum IgG and detectable levels of anti-PsaA IgA in saliva. Interestingly, immunization of C57BL/6 mice with PsaA alone or along with CTB did not result in detectable levels of either anti-PsaA IgG or IgA (data not shown), which is in accordance with our results previously obtained with BALB/c mice (1). The role of antibodies in protection against colonization is controversial.…”

supporting

confidence: 90%

“…It has been shown that PsaA has a significant role in protection against pneumococcal carriage, and it has been proposed for use as a component of a combined mucosal protein vaccine including PspA (7). More recently, we have described an increase in both systemic and mucosal antibodies in saliva and nasal and bronchial wash samples after intranasal immunization of mice with a cholera toxin B subunit (CTB)-PsaA fusion protein (1).…”

mentioning

confidence: 99%

“…Recombinant CTB and CTB-PsaA were obtained according to previously described methods (1,2). After 21 days, serum and saliva samples were analyzed in terms of IgG and IgA anti-PsaA production, respectively, through ELISA.…”

mentioning

confidence: 99%

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Intranasal Immunization with the Cholera Toxin B Subunit-Pneumococcal Surface Antigen A Fusion Protein Induces Protection against Colonization with Streptococcus pneumoniae and Has Negligible Impact on the Nasopharyngeal and Oral Microbiota of Mice

et al. 2006

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One of the candidate proteins for a mucosal vaccine antigen against Streptococcus pneumoniae is PsaA (pneumococcal surface antigen A). Vaccines targeting mucosal immunity may raise concerns as to possible alterations in the normal microbiota, especially in the case of PsaA, which was shown to have homologs with elevated sequence identity in other viridans group streptococci. In this work, we demonstrate that intranasal immunization with a cholera toxin B subunit-PsaA fusion protein is able to protect mice against colonization with S. pneumoniae but does not significantly alter the natural oral or nasopharyngeal microbiota of mice.

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confidence: 90%

mentioning

confidence: 99%

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Intranasal Immunization with the Cholera Toxin B Subunit-Pneumococcal Surface Antigen A Fusion Protein Induces Protection against Colonization with Streptococcus pneumoniae and Has Negligible Impact on the Nasopharyngeal and Oral Microbiota of Mice

et al. 2006

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“…ELISA plates were coated with 100 ng of S. frugiperda insect cell-derived VLPs diluted in PBS (assembled VLPs) or in 0.2 M carbonate buffer (pH 9.6) (disassembled VLPs) (23) at 4°C for 16 h. Pooled sera were tested for the presence of anti-L1 IgG as previously described (1). The titer was defined as the dilution at which the absorbance at 492 nm was 0.15.…”

mentioning

confidence: 99%

Production of Human Papillomavirus Type 16 L1 Virus-Like Particles by RecombinantLactobacillus caseiCells

Aires

Cianciarullo

Carneiro

et al. 2006

Appl Environ Microbiol

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Infections with human papillomavirus type 16 (HPV-16) are closely associated with the development of human cervical carcinoma, which is one of the most common causes of cancer death in women worldwide. At present, the most promising vaccine against HPV-16 infection is based on the L1 major capsid protein, which self-assembles in virus-like particles (VLPs). In this work, we used a lactose-inducible system based on the Lactobacillus casei lactose operon promoter (plac) for expression of the HPV-16 L1 protein in L. casei. Expression was confirmed by Western blotting, and an electron microscopy analysis of L. casei expressing L1 showed that the protein was able to self-assemble into VLPs intracellularly. The presence of conformational epitopes on the L. casei-produced VLPs was confirmed by immunofluorescence using the anti-HPV-16 VLP conformational antibody H16.V5. Moreover, sera from mice that were subcutaneously immunized with L. casei expressing L1 reacted with Spodoptera frugiperda-produced HPV-16 L1 VLPs, as determined by an enzymelinked immunosorbent assay. The production of L1 VLPs by Lactobacillus opens the possibility for development of new live mucosal prophylactic vaccines.

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“…Immunization of CTB and antigen fusion proteins resulted in strong antigen-specific mucosal response, 86 presumably by better antigen presentation through the B-subunit binding to antigen presenting cells. This is further supported by our recent work employing a pentameric single domain antibody (sdAb), or pentabody in vaccine development.…”

Section: Exploitation Of Bacterial Ab 5 Toxins As Mucosal Adjuvantsmentioning

confidence: 99%

Recent advances in the development of novel mucosal adjuvants and antigen delivery systems

Chen¹,

Patel²,

Yan³

et al. 2010

Human Vaccines

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Expression and characterization of cholera toxin B—pneumococcal surface adhesin A fusion protein in Escherichia coli: ability of CTB-PsaA to induce humoral immune response in mice

Cited by 58 publications

References 18 publications

Intranasal Immunization with the Cholera Toxin B Subunit-Pneumococcal Surface Antigen A Fusion Protein Induces Protection against Colonization with Streptococcus pneumoniae and Has Negligible Impact on the Nasopharyngeal and Oral Microbiota of Mice

Intranasal Immunization with the Cholera Toxin B Subunit-Pneumococcal Surface Antigen A Fusion Protein Induces Protection against Colonization with Streptococcus pneumoniae and Has Negligible Impact on the Nasopharyngeal and Oral Microbiota of Mice

Production of Human Papillomavirus Type 16 L1 Virus-Like Particles by RecombinantLactobacillus caseiCells

Recent advances in the development of novel mucosal adjuvants and antigen delivery systems

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