A Synthetic Peptide Homologous to Retroviral Transmembrane Envelope Proteins Depresses Protein Kinase C Mediated Lymphocyte Proliferation and Directly Inactivated Protein Kinase C: A Potential Mechanism for Immunosuppression

Kadota, Jun‐ichi; Cianciolo, George J.; Snyderman, Ralph

doi:10.1111/j.1348-0421.1991.tb01575.x

Cited by 31 publications

(12 citation statements)

References 48 publications

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“…CKS-17-BSA inhibited anti-SRBC plaque-forming cells (PFC) responses, secondary responses to tetanus toxoid as measured by ELISA and Con A-induced proliferation of cultured murine spleen cells. These results confirmed the findings of previous investigations (4,11,14,17,18,29,34,35). The suppressive effects of CKS-17-BSA were dose-dependent with less inhibition seen at lower dose of the conjugate.…”

Section: Resultssupporting

confidence: 95%

“…CKS-17-BSA has been shown to exert its effects by inactivating interleukin-1 (IL-1), interleukin-2 (IL-2), and IL-1-dependent IL-2 mediated responses through a mechanism involving protein kinase C (12,17,32). CKS-17-BSA also appears to act through inhibition of interferon-7 production (13,33).…”

Section: Discussionmentioning

confidence: 97%

“…This peptide, when conjugated to a carrier molecule, has been shown to specifically inhibit the function of multiple immune cells including ' '"'Present address: Division of AIDS, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland. 5Present address: Vacsyn S.A., Paris, France. lymphocytes (4,11,17,29,34), monocytes (13,14,18,35), and natural killer cells (15) in vitro. conjugates have also been shown to suppress cell-mediated immune responses in vivo (31).…”

Section: Introductionmentioning

confidence: 99%

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Modulation of the Immunosuppressive Activity of CKS-17, a Synthetic Retro viral Envelope Peptide, by Muramyl Dipeptide

et al. 1993

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CKS-17, a heptadecapeptide corresponding to a region highly conserved in retroviral transmembrane proteins is known to be immunosuppressive both in vitro and in vivo when conjugated to a carrier protein. Here we examined the effect of the synthetic adjuvant muramyl dipeptide (MDP) on the immunosuppressive properties of CKS-17-BSA in vitro. MDP was found to abrogate CKS-17-BSA-induced inhibition of both IgM plaque-forming cell responses and antitetanus toxin IgG secretion by BALB/c mouse spleen cells immunized in vivo and in vitro by sheep red blood cells and tetanus toxoid, respectively. In contrast, the CKS-17-BSA suppression of concanavalin A-induced splenocyte proliferation was not abrogated by MDP. The data suggest that muramyl peptides could be useful as immunoadjuvants for vaccines against retrovirus-associated immunosuppressive diseases.

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Section: Resultssupporting

confidence: 95%

Section: Discussionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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Modulation of the Immunosuppressive Activity of CKS-17, a Synthetic Retro viral Envelope Peptide, by Muramyl Dipeptide

et al. 1993

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“…Just N terminal to the transmembrane anchor sequence of the GP (residues 650 to 672) is a motif (residues 585 to 609) that is highly conserved in filoviruses. This sequence also has a high degree of homology with a motif in the glycoproteins of oncogenic retroviruses that has been shown to be immunosuppressive in vitro (8,17,19,23). Partially overlapping this motif is a heptad repeat sequence (53 residues; positions 541 to 593) that is thought to function in the formation of intermolecular coiled coils in the assembly of trimers, similar to structures predicted for the surface glycoproteins of other viruses (1,2).…”

mentioning

confidence: 77%

Biochemical Analysis of the Secreted and Virion Glycoproteins of Ebola Virus

Sanchez¹,

Yang

et al. 1998

J Virol

211

119

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The glycoproteins expressed by a Zaire species of Ebola virus were analyzed for cleavage, oligomerization, and other structural properties to better define their functions. The 50- to 70-kDa secreted and 150-kDa virion/structural glycoproteins (SGP and GP, respectively), which share the 295 N-terminal residues, are cleaved near the N terminus by signalase. A second cleavage event, occurring in GP at a multibasic site (RRTRR↓) that is likely mediated by furin, results in two glycoproteins (GP1 and GP2) linked by disulfide bonding. This furin cleavage site is present in the same position in the GPs of all Ebola viruses (R[R/K]X[R/K]R↓), and one is predicted for Marburg viruses (R[R/K]KR↓), although in a different location. Based on the results of cross-linking studies, we were able to determine that Ebola virion peplomers are composed of trimers of GP1-GP2 heterodimers and that aspects of their structure are similar to those of retroviruses, paramyxoviruses, and influenza viruses. We also determined that SGP is secreted from infected cells almost exclusively in the form of a homodimer that is joined by disulfide bonding.

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“…However, their function in the signal transduction leading to the cytokine modulation is unknown. For gammaretroviruses and HIV several signal transduction pathways were described and an inhibition of the protein kinase C by the isu peptide was shown [60]–[65]. The donor dependence suggests that genetic host factors (receptor polymorphism or differences in signal transduction?)…”

Section: Discussionmentioning

confidence: 99%

The Transmembrane Protein of the Human Endogenous Retrovirus - K (HERV-K) Modulates Cytokine Release and Gene Expression

2013

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Numerous copies of endogenous retroviruses are present in the genome of mammals including man. Although most of them are defective, some, e.g., the human endogenous retroviruses HERV-K, were found to be expressed under certain physiological conditions. For instance, HERV-K is expressed in germ cell tumours and melanomas as well as in the placenta. Most exogenous retroviruses including the human immunodeficiency virus HIV-1 induce severe immunodeficiencies and there is increasing evidence that the transmembrane envelope (TM) proteins of these retroviruses may be involved. We show here that HERV-K particles released from a human teratocarcinoma cell line, a recombinant TM protein and a peptide corresponding to a highly conserved so-called immunosuppressive domain in the TM protein of HERV-K inhibit the proliferation of human immune cells, induce modulation of the expression of numerous cytokines, and modulate the expression of cellular genes as detected by a microarray analysis. The changes in cytokine release and gene expression induced by the TM protein of HERV-K are similar to those found previously induced by the TM protein of HIV-1. These data suggest that the mechanism of immunosuppression may be similar for different retroviruses and that the expression of the TM protein in tumours and in the placenta may suppress immune responses and thus prevent rejection of the tumour and the embryo.

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A Synthetic Peptide Homologous to Retroviral Transmembrane Envelope Proteins Depresses Protein Kinase C Mediated Lymphocyte Proliferation and Directly Inactivated Protein Kinase C: A Potential Mechanism for Immunosuppression

Abstract: CKS-

Cited by 31 publications

References 48 publications

Modulation of the Immunosuppressive Activity of CKS-17, a Synthetic Retro viral Envelope Peptide, by Muramyl Dipeptide

Modulation of the Immunosuppressive Activity of CKS-17, a Synthetic Retro viral Envelope Peptide, by Muramyl Dipeptide

Biochemical Analysis of the Secreted and Virion Glycoproteins of Ebola Virus

The Transmembrane Protein of the Human Endogenous Retrovirus - K (HERV-K) Modulates Cytokine Release and Gene Expression

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