Immunogenicity of a fusion protein linking the beta subunit carboxyl terminal peptide (CTP) of human chorionic gonadotropin to the B subunit of Escherichia coli heat-labile enterotoxin (LTB)

Rock, Edwin P.; Reich, Karl; Lyu, D.M.; Hovi, Marianne; Hardy, Jonathan; Schoolnik, Gary K.; Stocker, B. A. D.; Stevens, Vernon C.

doi:10.1016/s0264-410x(96)00046-1

Cited by 9 publications

(4 citation statements)

References 40 publications

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“…A similar ability of the fusion protein antisera to detect native as well fusion partners has been demonstrated in earlier studies (Bhatia et al 2014; Sharma and Dixit 2015). Studies have also shown that LTB when used as an adjuvant could generate a strong immune response towards the fused antigens (Pillai et al 1996; Rock et al 1996; Marchioro et al 2014).…”

Section: Discussionmentioning

confidence: 99%

Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D

et al. 2019

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Epsilon toxin (Etx) produced by Clostridium perfringens types B and D, a major causative agent of enterotoxaemia causes significant economic losses to animal industry. Conventional vaccines against these pathogens generally employ formalin-inactivated culture supernatants. However, immunization with the culture supernatant and full length toxin subjects the animal to antigenic load and often have adverse effect due to incomplete inactivation of the toxins. In the present study, an epitope-based vaccine against Clostridium perfringens Etx, comprising 40–62 amino acid residues of the toxin in translational fusion with heat labile enterotoxin B subunit (LTB) of E. coli , was evaluated for its protective potential. The ability of the fusion protein rLTB.Etx 40–62 to form pentamers and biologically active holotoxin with LTA of E. coli indicated that the LTB present in the fusion protein retained its biological activity. Antigenicity of both the components in the fusion protein was retained as anti-fusion protein antisera detected both the wild type Etx and LTB in Western blot analysis. Immunization of BALB/c mice with the fusion protein resulted in a significant increase in all isotypes, predominantly IgG1, IgG2a and IgG2b. Anti-fusion protein antisera neutralized the cytotoxicity of epsilon toxin both in vitro and in vivo. Thus, the results demonstrate the potential of rLTB.Etx 40–62 as a candidate vaccine against C. perfringens . Electronic supplementary material The online version of this article (10.1186/s13568-019-0824-3) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D

et al. 2019

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“…The ease of HLTs genetic manipulation can be exploited to engineer chimeras with HIV epitopes either by using their non-toxic B subunits or modified holotoxins that have reduced or no toxicity. Both strategies have been proven successful with a number of proteins [ 37 – 40 ]. For LT-I, these include fusing an epitope of the Bordetella pertussis p69 antigen to LT-IB [ 39 ].…”

Section: E Coli Heat-labile Enterotoxins As Potential Adjuvmentioning

confidence: 99%

he Quest for an HIV-1 Vaccine Adjuvant: Bacterial Toxins as New Potential Platforms

Nashar¹

2014

J Clin Cell Immunol

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While tremendous efforts are undergoing towards finding an effective HIV-1 vaccine, the search for an HIV-1 vaccine adjuvant lags behind and is understudied. More recently, however, efforts have focused on testing adjuvant formulations that can boost the immune response and generate broadly neutralizing antibodies to HIV-1 ENV (gp160). Despite this, there remain a number of challenges towards achieving this goal. These include safety of adjuvant formulations; stability of the incorporated antigens; maintenance of ENV immunogenicity; optimal inoculation sites; the effective combination of adjuvants; stability of ENV neutralizing epitopes in some adjuvant formulations; mucosal immunity; and long-term maintenance of the immune response. A new class of adjuvants for HIV-1 proteins is suggested to overcome many of the limitations of some other adjuvants. Type 1 (LT-I) and type 2 (LT-II) human E. coli enterotoxins (HLTs) and their non-toxic B-subunits derivatives are strong systemic and mucosal adjuvants and effective carriers for other proteins and epitopes. Their stable molecular structure in the presence of fused proteins and epitopes, and their ability to target surface receptors on antigen presenting cells make them ideal for the delivery of HIV-1 ENV or HIV other proteins. Importantly, unlike some other adjuvants, HLTs and derivatives have well-defined modes of immune system activation. The challenges in finding optimal HIV-1 vaccine adjuvant formulation and the important properties of HLTs are discussed.

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“…Immunization of mice with the purified recombinant LTB-CTP protein without any additional adjuvants led to generation of hCG-specific antibody responses [104]. In rabbits, a single injection of CTP of b-hCG cosynthesized with a T-cell epitope from tetanus toxoid (TT) and entrapped in polymer microspheres elicited strong antibody response with equivalent duration to that of a three-injection schedule delivered by water-in-oil emulsion [105].…”

Section: B-hcg Vaccine Based On Ctpmentioning

confidence: 99%

Vaccines for immunological control of fertility

Gupta

Bansal

2009

Reprod Medicine & Biology

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Vaccines have been proposed as one of the strategies for population control. Immunocontraceptive vaccines can be designed to inhibit: (1) production of gametes (sperm and egg); (2) functions of gametes, leading to blocking of fertilization; and (3) gamete outcome (pregnancy). Immunization with gonadotropin-releasing hormone coupled to different carriers has shown curtailment in the production of sperm with concomitant infertility in various species. Immunization of nonhuman primates and men with ovine follicle stimulating hormone has also resulted in reduced sperm output. Various spermatozoa-specific proteins such as FA1, PH-20, LDH-C, SP-10, SP-17, sp56, SPAG9, and Izumo have been proposed as candidate antigens to develop contraceptive vaccines, which have shown efficacy in inhibiting fertility in different animal models. Immunization with zona pellucida glycoproteins-based immunogens also results in curtailment of fertility in a variety of species. However, ways to overcome the observed oophoritis associated with zona proteins immunization have yet to be discovered, a necessary step before their proposal for control of human population. Nonetheless, this is a very promising approach to control wildlife animal population. Phase II clinical trials of β-human chorionic gonadotropin-based vaccine in women have established the proof of principle that it is possible to inhibit fertility without any untoward side-effects by vaccination. Further scientific inputs are required to increase the efficacy of contraceptive vaccines and establish their safety beyond doubt, before they can become applicable for control of fertility in humans.

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Immunogenicity of a fusion protein linking the beta subunit carboxyl terminal peptide (CTP) of human chorionic gonadotropin to the B subunit of Escherichia coli heat-labile enterotoxin (LTB)

Cited by 9 publications

References 40 publications

Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D

Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D

he Quest for an HIV-1 Vaccine Adjuvant: Bacterial Toxins as New Potential Platforms

Vaccines for immunological control of fertility

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