Inducing systemic and mucosal immune responses to B-T construct of F1 antigen of Yersinia pestis in microsphere delivery

Tripathi, Vinita; Keisham, Chitralekha; Bakshi, A.; Tomar, Deepak; Deshmukh, Ranjana; Baig, Masroor A.; Rao, D. N.

doi:10.1016/j.vaccine.2006.01.031

Cited by 34 publications

(39 citation statements)

References 38 publications

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“…Although this self-association is due mainly to the F1 subcomponent, the fusion architecture actually reduces polydispersity compared to the individual F1 protein, which is even more aggregative [6]. Thus, the F1-V fusion based plague antigen is at the forefront of plague vaccine development [23][24][25][26]. As demonstrated by the findings reported herein, we propose that use of the described F1-V C424S protein form should facilitate the enhanced production and stability of F1-V-based plague vaccines.…”

Section: Discussionmentioning

confidence: 99%

Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague

Goodin

Nellis

Powell

et al. 2007

Protein Expression and Purification

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The F1-V vaccine antigen, protective against Yersinia pestis, exhibits a strong tendency to multimerize that affects larger-scale manufacture and characterization. In this work, the sole F1-V cysteine was replaced with serine by site-directed mutagenesis for characterization of F1-V noncovalent multimer interactions and protective potency without participation by disulfide-linkages. F1-V and F1-V C424S proteins were over-expressed in Escherichia coli, recovered using mechanical lysis/pH-modulation and purified from urea-solubilized soft inclusion bodies, using successive ionexchange, ceramic hydroxyapatite, and size-exclusion chromatography. This purification method resulted in up to 2 mg per gram of cell paste of 95% pure, mono-disperse protein having ≤ 0.5 endotoxin units per mg by a kinetic chromogenic limulus amoebocyte lysate reactivity assay. Both F1-V and F1-V C424S were monomeric at pH 10.0 and progressively self-associated as pH conditions decreased to pH 6.0. Solution additives were screened for their ability to inhibit F1-V self-association at pH 6.5. An L-arginine buffer provided the greatest stabilizing effect. Conversion to >500-kDa multimers occurred between pH 6.0 and 5.0. Conditions for efficient F1-V adsorption to the cGMPcompatible Alhydrogel® adjuvant were optimized. Side-by-side evaluation for protective potency against subcutaneous plague infection in mice was conducted for F1-V C424S monomer; cysteinecapped F1-V monomer; cysteine-capped F1-V multimer; and a F1-V standard reported previously. After a two-dose vaccination with 2 × 20 µg of F1-V, respectively, 100, 80, 80, and 70% of injected mice survived a subcutaneous lethal plague challenge with 10 8 LD 50 Y. pestis CO92. Thus, vaccination with F1-V monomer and multimeric forms resulted in significant, and essentially equivalent, protection.

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Section: Discussionmentioning

confidence: 99%

Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague

Goodin

Nellis

Powell

et al. 2007

Protein Expression and Purification

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“…Synthetic peptides corresponding to Bcell epitopes have shown promise as vaccines for combating pathogenic infections. Recently, synthetic peptide vaccines have been tested against coronavirus (He et al, 2006), human immunodeficiency virus 1 (Cruz et al, 2009), influenza A virus (Wang et al, 2010), Toxoplasma gondii (Tan et al, 2010), and Yersinia pestis (Tripathi et al, 2006;Khan et al, 2008). Therefore, to determine the B-cell epitope of EV70 is an important step in developing a peptide vaccine for EV70.…”

Section: Introductionmentioning

confidence: 99%

A peptide vaccine based on a B-cell epitope on the VP1 protein of enterovirus 70 induces a strong antibody response

Park¹,

Lim²,

Ye³

et al. 2012

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Summary. -Enterovirus 70 (EV70) is the causative agent of acute hemorrhagic conjunctivitis (AHC), for which no effective vaccine is available. This study revealed a high reactivity of the N-terminal region of EV70 VP1 (VP1-1) with an anti-EV70 mouse serum. The analysis of overlapping synthetic peptides of VP1-1 identified a B-cell epitope in this region. The E-peptide (14-ANTVESEIKAELGVI-28) showing the highest reactivity with the anti-EV70 serum induced neutralizing antibodies in mice and reduced the virus titer in the eyes, suggesting that it is a candidate vaccine against AHC caused by EV70.Keywords: enterovirus 70; AHC; B-cell epitope; peptide vaccine * Corresponding author. E-mail: jhnam@catholic.ac.kr; phone: +82-2-2164-4917. # These authors contributed equally to this work. Abbreviations: EV70 = enterovirus 70; AHC = acute hemorrhagic conjunctivitis; VP1-1 = virus capsid protein VP1 amino-terminus; VP1-2 = virus capsid protein VP1 middle; VP1-3 = virus capsid protein carboxy-terminus

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“…Although these vaccines have several shortcomings, evidences indicate that protection against both bubonic and pneumonic forms of plague can be achieved [30]. To overcome the drawbacks of the presently available vaccines, a number of researchers are working toward the development of improved vaccines using different strategies like recombinant or peptide-based immunogens [5,9,37,44,46]. Presently, it is understood that using F1 or V or both as a subunit vaccine will be more beneficial than attenuated or killed whole cell vaccines.…”

Section: Introductionmentioning

confidence: 99%

“…Earlier studies from our laboratory on F1 antigen demonstrated complete in vivo protection of two B-T constructs using PLGA microspheres/liposomes as delivery vehicles through intranasal and intramuscular routes of immunization [31,32,37]. Again, toward developing peptide-based vaccine using V antigen, different B-and T-cell epitopes were mapped, humoral, cellular and mucosal immune response were studied using intramuscular as well as intranasal routes of immunization [20].…”

Section: Introductionmentioning

confidence: 99%

Humoral immune responses and protective efficacy of sequential B- and T-cell epitopes of V antigen of Yersinia pestis by intranasal immunization in microparticles

Uppada

Khan

Bhat

et al. 2009

Med Microbiol Immunol

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Capsular F1 and secretory V antigen are the putative vaccine candidates for plague, caused by Yersinia pestis. Contemplating this, we studied the immunogenicity and protective efficacy of collinearly synthesized B- and T-cell epitopes (B-T constructs) of V antigen entrapped in poly (DL-lactide-co-glycolide) microparticles immunized intranasally using single dose immunization schedule in outbred, H-2(b) and H-2(d) mice. High antibody levels were observed in terms of IgG, IgA and SIgA peak titers in sera and mucosal washes to different B-T constructs. The constructs ai, bi and fi especially showed high peak antibody titers ranging from 51,200 to 204,000, which were maintained till day 120 post immunization. IgG/IgA Specific activity in sera and washes correlated well with the peak antibody titers. Moreover, all the B-T constructs showed mixed IgG1 and IgG2a/2b response, variable immunoreactivity as well as memory response with V antigen. B-T constructs, viz ai, ak, bi, fi, di and ik showed comparatively high isotype levels. These constructs showed high immunoreactivity, and good recall response with V antigen. Finally, in vivo protective study in BALB/c mice demonstrated the protective efficacy of three B-T constructs (ai, bi and fi) against lethal doses of Yersinia pestis till day 20 post challenge, while construct 'id' showed partial protection.

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Inducing systemic and mucosal immune responses to B-T construct of F1 antigen of Yersinia pestis in microsphere delivery

Cited by 34 publications

References 38 publications

Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague

Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague

A peptide vaccine based on a B-cell epitope on the VP1 protein of enterovirus 70 induces a strong antibody response

Humoral immune responses and protective efficacy of sequential B- and T-cell epitopes of V antigen of Yersinia pestis by intranasal immunization in microparticles

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