Lymphocyte Proliferation Induced by Pertusis Toxin Utilizes a Pathway Parallel to Transforming Growth Factor-Beta-Sensitive Growth

Cronkhite, R

doi:10.1159/000236564

Cited by 3 publications

(2 citation statements)

References 10 publications

(13 reference statements)

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“…Studies in the mouse using ZP3 peptide has suggested that cytotoxic T cells may be involved in oocyte damage [Rhim et al, 1992;Lou and Tung, 1993]. Many of these studies have utilized the pertussis toxoid in foot pad injections which has been shown to be a molecular mimic that itself induces autoimmune disease [Cronkhite, 1993;Sudweeks et al, 1993;Ryan et al, 1998], making this a complicated model system to study ZP immune response. However, Paterson et al [1998] have demonstrated suppression of fertility in marmosets that were administered with human ZP3 peptide immunogen without any effect on follicular development.…”

Section: Effect Of Antibodies Against Zp Proteins On Ovarian Folliculmentioning

confidence: 99%

Structure and Function of the Proteins of the Mammalian Zona pellucida

Prasad¹,

Skinner²,

Cariño³

et al. 2000

Cells Tissues Organs

101

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The zona pellucida (ZP) is the extracellular matrix that plays important roles in sperm-egg interaction. The ZP is composed of three major glycoproteins that exhibit heterogeneity due to extensive post-translational modifications including glycosylation and sulfation. Because of these modifications the nomenclature of ZP proteins from different species based on electrophoretic mobilities has been confusing. As the cDNAs and genes encoding the different ZP proteins have been isolated and sequenced, it is now possible to relate these ZP proteins according to gene families. Using the mouse ZP nomenclature, the ZP proteins from different mammalian species can be classified into three protein families: ZP1, ZP2, and ZP3. Although some of the structural domains of the ZP proteins of different species are conserved within each family, they exhibit distinct biological properties. In the mouse it has been established that ZP3 is the primary sperm receptor while ZP2 has secondary sperm receptor properties. In the pig, however, ZP1 has been shown to have sperm receptor activity similar to that observed in the rabbit and nonhuman primates. It is of interest that the human ZP2 and ZP3 gene families are 60–70% conserved with respect to the mouse ZP amino acid sequence, while the mouse ZP1 is only 39% conserved with respect to human ZP1. Such differences in protein structure and glysosylation may explain the marked species differences in the biochemical, physicochemical and immunochemical properties of the ZP. Studies have now shown that the proteins of the ZP are expressed in a stage specific manner and that there is increasing evidence that ZP proteins are expressed by both granulosa cells and the oocyte and may play a role in granulosa cell differentiation.

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Section: Effect Of Antibodies Against Zp Proteins On Ovarian Folliculmentioning

confidence: 99%

Structure and Function of the Proteins of the Mammalian Zona pellucida

Prasad¹,

Skinner²,

Cariño³

et al. 2000

Cells Tissues Organs

101

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show abstract

“…pertussis infection or administration of a whole-cell based B. pertussis vaccine have been shown to induce Agspecific IFN-γ production from both CD4 + and CD8 + T cells and Th1 responses in infants [62]. Indeed, PTX has been widely used to induce Th1-mediated organ-specific experimental autoimmune (EA) diseases in animal models, including murine encephalomyelitis (EAE), orchitis and uveitis (EAU) [63][64][65][66][67][68][69]. In particular, EAU was shown to be mediated by the expression of IFN-γ from PTX-stimulated dendritic cells (DC) [39], although transfer of lymphocytes from PTX-treated donor mice could cause this disease [70].…”

Section: Ptx/ptx-b Modulation Of Autoimmune Responsesmentioning

confidence: 99%

Immunomodulatory and Anti-Viral Activities of Pertussis Toxin and of Its Non-Toxic Derivatives

Alfano

Poli

2005

CMCAIAA

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The innate immune system represents the fastest defense to microbial invasion although many pathogens can modulate the host response either in favor of or against their survival and propagation. In this regard, some bacterial toxins possess immunostimulating properties that have been exploited in terms of vaccine adjuvancy and induction of specific cytotoxic T lymphocytes. Among these, Bordetella pertussis toxin (PTX) possesses the ability of modulating the immune responses in in vivo, ex-vivo and in vitro experimental systems. In addition, PTX, as well its nontoxic B-oligomer PTX-B and the genetically inactivated PT-9K/129G molecule, have been recently shown to inhibit infection of CD4 + T lymphocytes and macrophages by the human immunodeficiency virus, the etiological agent of the acquired immunodeficiency syndrome. This article focuses on the regulation of the immune response and on the anti-viral properties of PTX and of its nontoxic related molecules and as an example of exploitation of a natural bacterial product to combat viral infections.

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Mapping of Dominant B-Cell Epitopes of a Human Zona Pellucida Protein (ZP1)1

Skinner

Schwoebel

Prasad

et al. 1999

Biology of Reproduction

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Zona pellucida (ZP) glycoproteins contain numerous antigenic determinants including carbohydrate, protein, and conformational epitopes; and the immunogenicity of these complex glycoproteins varies in different mammalian hosts. Studies have now shown that antibodies from primates immunized with a cDNA-expressed recombinant rabbit ZP protein (the homologue of the human ZP1 [hZP1]) inhibit sperm binding to the ZP without altering ovarian function, unlike immunization with ZP3 and ZP2 protein families. The ZP1 protein or peptides derived from it (recombinant or synthetic) are therefore primary candidates for use in designing safe and reversible human and animal contraceptive vaccines. In order to define peptide epitope(s) that may be critical for eliciting an immune response sufficient to effect immunological contraception without causing any adverse effects on ovarian physiology, studies have been carried out to identify immunodominant B-cell epitopes of the ZP1 protein. The amino acid sequence of the hZP1 was used to design a set of 94 (15-mer) biotinylated peptides having an overlap of 9 amino acids. Using these peptides in a modified enzyme-linked immunoassay, antibodies in sera from rabbits or baboons immunized with native porcine ZP protein were screened for ZP1 peptide recognition. These studies demonstrate that there are a limited number of peptides recognized by primate antibodies but that the overlapping peptides sharing the sequence GPLTLELQI are recognized by both rabbit and baboon antibodies regardless of the adjuvant system used to induce the immune response. This peptide is 100% conserved in amino acid sequence between the human and pig, although the rabbit protein has two conserved amino acid substitutions (100% similar, 77% identical). Because this peptide is immunogenic as well as antigenic in primates, it could play a major role in the development of human contraceptive vaccines.

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Lymphocyte Proliferation Induced by Pertusis Toxin Utilizes a Pathway Parallel to Transforming Growth Factor-Beta-Sensitive Growth

Cited by 3 publications

References 10 publications

Structure and Function of the Proteins of the Mammalian Zona pellucida

Structure and Function of the Proteins of the Mammalian Zona pellucida

Immunomodulatory and Anti-Viral Activities of Pertussis Toxin and of Its Non-Toxic Derivatives

Mapping of Dominant B-Cell Epitopes of a Human Zona Pellucida Protein (ZP1)1

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