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Pfizer Inc mason pfizer monkey virus
Mason Pfizer Monkey Virus, supplied by Pfizer Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mason+pfizer+monkey+virus/mason+monkey+pfizer+virus/pm42278261-146-26-26
Average 86 stars, based on 1 article reviews

mason pfizer monkey virus - by Bioz Stars, 2026-09

86/100 stars

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Retroviral:

Article Title: Transcription start site heterogeneity controls MDA5 sensing of unspliced HIV-1 RNAs.
Article Snippet: .. We next determined if Rev/CRM1 export was strictly necessary for cap1G usRNA-driven interferon responses, as we and others have previously shown that substitution of Rev/CRM1 usRNA export with a retroviral constitutive transport element (CTE) from Mason-Pfizer Monkey Virus (a betaretrovirus) fails to induce innate immune responses (22, 23). ..

Virus:

Article Title: Further Evidence for the Immunosuppressive Activity of Transmembrane Envelope Protein p15E of Porcine Endogenous Retrovirus.
Article Snippet: [CrossRef] [PubMed] 24. .. Blaise, S.; Mangeney, M.; Heidmann, T. The envelope of Mason-Pfizer monkey virus has immunosuppressive properties. ..

Article Title: ZNF638 represses the transcription of HBV closed circular DNA involving HUSH complex-mediated histone modifications of epigenetic silencing
Article Snippet: .. There is also a report suggesting that ZNF638 suppressed the expression from unintegrated genomes of HIV-1 and Mason-Pfizer monkey virus without the involvement of the HUSH complex [ ]. ..

Article Title: Dissection of the EIAV Core Packaging Region Identifies SL2 Stem and SL2-SL3 Junction as Gag-Associated Packaging Determinants and Antiviral Targets.
Article Snippet: .. Meanwhile, the enrichment of unpaired guanosines within the SL2-SL3 junction mirrors the specific NC-guanine interactions observed in HIV-1 and is reminiscent of the purine-rich linkers in Mason-Pfizer Monkey Virus [42,43]. ..

Article Title: Transient inhibition of p53 in gene therapy
Article Snippet: .. Alternatively, a constitutive transport element from certain simple retroviruses such as Mason-Pfizer monkey virus can be used to relieve the requirement for Rev and RRE. ..

Article Title: Mechanisms of HIV Latency in Hematopoietic Progenitors: GFI1 as a Key Regulator
Article Snippet: .. Similarly, ZFP961, another murine KRAB zinc finger protein, can inhibit Mason-Pfizer monkey virus (which utilizes the tRNA Lys 1,2 PBS [PBS-Lys1,2]) as well as HIV (which uses the Lys3 tRNA PBS [PBS-Lys3] in the HIV LTR) . ..

Article Title: ZNF638 represses the transcription of HBV closed circular DNA involving HUSH complex-mediated histone modifications of epigenetic silencing.
Article Snippet: .. There is also a report suggesting that ZNF638 suppressed the expression from unintegrated genomes of HIV-1 and Mason-Pfizer monkey virus without the involvement of the HUSH complex [22]. ..

Article Title: Further Evidence for the Immunosuppressive Activity of Transmembrane Envelope Protein p15E of Porcine Endogenous Retrovirus.
Article Snippet: .. This was shown for p15E of MoMuLV [23], the transmembrane envelope proteins of Mason-Pfizer monkey virus [24], human endogenous retrovirus-H (HERV-H) [25], FeLV [26], and one of two murine and one of two human syncytins [27]. ..

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SDS-PAGE and immunoblot analysis of cross-linked MA-CaM complexes . The mixture of CaM and myrMAPP as well as individual proteins were treated with DSBU and DSPU cross-linkers at increasing molar excesses of cross-linker to protein (5-fold molar excess and 10-fold molar excess) and analyzed by SDS-PAGE with Coomassie detection ( left panels ) or with immunoblot detection by the use of antibodies against M-PMV MA ( middle panels ) or against CaM ( right panels ). Individual proteins were detected as signals of ∼14.4 kDa (myrMAPP; illustrated by a gray circle ) and ∼17 kDa (CaM; illustrated by a blue square) which corresponds to their molecular weight (14.9 kDa of myrMAPP and 16.7 kDa of CaM). In mixed samples of myrMAPP and CaM, additional bands of higher molecular weight appear upon cross-linker treatment, indicating formation of oligomeric CaM–myrMAPP complexes. Data shown are representative of two independent biological replicates.

Journal: The Journal of Biological Chemistry

Article Title: Structural and functional insights into calmodulin-mediated lipid binding and proteolytic cleavage of the M-PMV matrix protein

doi: 10.1016/j.jbc.2025.111102

Figure Lengend Snippet: SDS-PAGE and immunoblot analysis of cross-linked MA-CaM complexes . The mixture of CaM and myrMAPP as well as individual proteins were treated with DSBU and DSPU cross-linkers at increasing molar excesses of cross-linker to protein (5-fold molar excess and 10-fold molar excess) and analyzed by SDS-PAGE with Coomassie detection ( left panels ) or with immunoblot detection by the use of antibodies against M-PMV MA ( middle panels ) or against CaM ( right panels ). Individual proteins were detected as signals of ∼14.4 kDa (myrMAPP; illustrated by a gray circle ) and ∼17 kDa (CaM; illustrated by a blue square) which corresponds to their molecular weight (14.9 kDa of myrMAPP and 16.7 kDa of CaM). In mixed samples of myrMAPP and CaM, additional bands of higher molecular weight appear upon cross-linker treatment, indicating formation of oligomeric CaM–myrMAPP complexes. Data shown are representative of two independent biological replicates.

Article Snippet: The matrix (MA) domain of the Mason-Pfizer monkey virus (M-PMV) Gag polyprotein plays a central role in retroviral assembly and trafficking, coordinating membrane association and proteolytic maturation.

Techniques: SDS Page, Western Blot, Molecular Weight

Co-immunoprecipitation of M-PMV Gag and HA-tagged CaM in HEK293T cells . HEK293T cells were co-transfected with plasmids encoding non-infectious M-PMV (pSARM4 RT) and HA-tagged human CaM (pCMV HA-CaM). Cell lysates were subjected to co-immunoprecipitation using anti-HA magnetic agarose beads (Chromotek HA-trap). Anti-MA antibody (1:2500) was used for immunoblot detection. The binding of HA-CaM was inspected by immunoblot using anti CaM antibody. Note, the bottom band is a nonspecific signal that was also detected in the mock sample of non-transfected cells (see ). Data shown are representative of three independent biological replicates.

Journal: The Journal of Biological Chemistry

Article Title: Structural and functional insights into calmodulin-mediated lipid binding and proteolytic cleavage of the M-PMV matrix protein

doi: 10.1016/j.jbc.2025.111102

Figure Lengend Snippet: Co-immunoprecipitation of M-PMV Gag and HA-tagged CaM in HEK293T cells . HEK293T cells were co-transfected with plasmids encoding non-infectious M-PMV (pSARM4 RT) and HA-tagged human CaM (pCMV HA-CaM). Cell lysates were subjected to co-immunoprecipitation using anti-HA magnetic agarose beads (Chromotek HA-trap). Anti-MA antibody (1:2500) was used for immunoblot detection. The binding of HA-CaM was inspected by immunoblot using anti CaM antibody. Note, the bottom band is a nonspecific signal that was also detected in the mock sample of non-transfected cells (see ). Data shown are representative of three independent biological replicates.

Techniques: Immunoprecipitation, Transfection, Western Blot, Binding Assay

$Model of myrMAPP-CaM complex . A , structure of HIV-1 MA(8–43)-CaM complex published by Vlach et al . (PDB entry 2mgu) . CaM is colored in cyan , HIV-1 MA(8–43) in magenta and calcium ions in red . NTD – N-terminal domain, CTD – C-terminal domain. B , NMR chemical shift changes and differential HDX relative fractional uptake detected for CaM interacting with M-PMV myrMAPP mapped onto the published structure of free CaM and CaM in complex with HIV-1 MA(8–43) . Free CaM (PDB 1Cll) is shown on the left , and CaM, as observed in the complex with HIV-1 MA(8–43) on the right , both colored according to our M-PMV myrMAPP interaction results. Top panels : NMR chemical shifts, with residues showing shifts in orange and residues without detectable shifts in cyan . Bottom panels : Differential HDX relative fractional uptake, where differential deuterium uptake at 20 s is indicated by the intensity of blue coloring. C , structure of M-PMV MAPP ( gray ) in complex with CaM (cyan) calculated by HADDOCK with visualized identified cross-links between myrMAPP and CaM. Cross-links meeting the maximal distance of 35 Å are depicted as green dashes, cross-links exceeding the maximum distance of 35 Å are depicted as red dash. D , structure of M-PMV myrMAPP ( gray ) in complex with CaM ( cyan ) calculated by HADDOCK with visualized chemical shifts detected by NMR. Residues with chemical shifts detected in equimolar ratio of proteins in the analyzed myrMAPP sample are colored in orange , whereas those detected in the sample with increased concentration of CaM (1:5) are colored in blue , which also comprises the orange residues. E , structure of M-PMV MAPP in complex with CaM calculated by HADDOCK with visualized differential HDX relative fractional uptake. Degree of deuteration is shown as intensity of blue and red color. F , structure of M-PMV MAPP ( gray ) in complex with CaM ( cyan ) calculated by HADDOCK with visualized individual functional regions of MA. Residues in MA involved in MA oligomerization are colored in yellow ( , ), residues interacting with PI(4,5)P 2 are shown in magenta , residues interacting with the M-PMV cytotail are colored in green . Additionally, residue that interacts with both the M-PMV cytotail and PI(4,5)P 2 is colored blue and residue that interacts with the cytotail and also involved in oligomerization is colored in red .$

Journal: The Journal of Biological Chemistry

Article Title: Structural and functional insights into calmodulin-mediated lipid binding and proteolytic cleavage of the M-PMV matrix protein

doi: 10.1016/j.jbc.2025.111102

Figure Lengend Snippet: Model of myrMAPP-CaM complex . A , structure of HIV-1 MA(8–43)-CaM complex published by Vlach et al . (PDB entry 2mgu) . CaM is colored in cyan , HIV-1 MA(8–43) in magenta and calcium ions in red . NTD – N-terminal domain, CTD – C-terminal domain. B , NMR chemical shift changes and differential HDX relative fractional uptake detected for CaM interacting with M-PMV myrMAPP mapped onto the published structure of free CaM and CaM in complex with HIV-1 MA(8–43) . Free CaM (PDB 1Cll) is shown on the left , and CaM, as observed in the complex with HIV-1 MA(8–43) on the right , both colored according to our M-PMV myrMAPP interaction results. Top panels : NMR chemical shifts, with residues showing shifts in orange and residues without detectable shifts in cyan . Bottom panels : Differential HDX relative fractional uptake, where differential deuterium uptake at 20 s is indicated by the intensity of blue coloring. C , structure of M-PMV MAPP ( gray ) in complex with CaM (cyan) calculated by HADDOCK with visualized identified cross-links between myrMAPP and CaM. Cross-links meeting the maximal distance of 35 Å are depicted as green dashes, cross-links exceeding the maximum distance of 35 Å are depicted as red dash. D , structure of M-PMV myrMAPP ( gray ) in complex with CaM ( cyan ) calculated by HADDOCK with visualized chemical shifts detected by NMR. Residues with chemical shifts detected in equimolar ratio of proteins in the analyzed myrMAPP sample are colored in orange , whereas those detected in the sample with increased concentration of CaM (1:5) are colored in blue , which also comprises the orange residues. E , structure of M-PMV MAPP in complex with CaM calculated by HADDOCK with visualized differential HDX relative fractional uptake. Degree of deuteration is shown as intensity of blue and red color. F , structure of M-PMV MAPP ( gray ) in complex with CaM ( cyan ) calculated by HADDOCK with visualized individual functional regions of MA. Residues in MA involved in MA oligomerization are colored in yellow ( , ), residues interacting with PI(4,5)P 2 are shown in magenta , residues interacting with the M-PMV cytotail are colored in green . Additionally, residue that interacts with both the M-PMV cytotail and PI(4,5)P 2 is colored blue and residue that interacts with the cytotail and also involved in oligomerization is colored in red .

Techniques: Concentration Assay, Functional Assay, Residue

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