Disease relevance of Psmd1

• Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope [1].
• With the use of reassortant viruses containing various combinations of double-stranded RNA segments (genes) derived from type 1 and type 3, the viral S1 double-stranded RNA segment was shown to be responsible for determining the capacity of reoviruses to spread to the central nervous system through these distinct pathways [2].
• Transgenic mice expressing the influenza virus PR8 hemagglutinin I-Ed-restricted determinant S1 (HA Tg mice) mediate negative selection of PR8 S1-specific T cells, but respond to immunization with a virus containing a closely related analogue, S1(K113) [3].
• We conclude that reovirus type 1 infection can lead to polyendocrinopathy and autoimmunity and that the S1 gene segment is required for the induction of autoantibodies to GH [4].
• Toward the development of a safe, effective, and inexpensive vaccine candidate, we have expressed the N-terminal fragment of SARS-CoV S protein (S1) in tomato and low-nicotine tobacco plants [5].

High impact information on Psmd1

• Following the establishment of persistent infection, mutations in the S1 gene appeared in two of three cell lines [6].
• Amino acid residues 8 to 15 of PTX subunit S1 are important for the adenosine diphosphate-ribosyltransferase activity associated with the pathobiological effects of PTX [1].
• Decoration with subfragment 1 (S1) of myosin confirmed that relatively few actin filaments travel horizontally in the web [7].
• Incorporation of the S1 fragment into plant genomes as well as its transcription was confirmed by PCR and RT-PCR analyses [5].
• Prior studies have determined that the localization of virus in different cell types in the brain (tropism) is a property of the viral hemagglutinin, the product of the S1 RNA genome segment [8].

Chemical compound and disease context of Psmd1

• Growth of reassortant viruses in ammonium chloride-treated cells segregated with the S1 gene of L/C and the S4 gene of PI 2A1 and PI 3-1 [9].
• The cleavage products of the spike (S) protein, the S1 and S2 subunits, of the highly neurovirulent murine coronavirus (MHV) JHMV c1-2 variant were identified by immunoprecipitation of virus-infected cell lysates after treatment with urea and 2-mercaptoethanol [10].
• Pertussis toxin, with lysine substituted for arginine at position 9 in the S1 subunit (PTA-K9) was assembled and expressed to wild type levels [11].

Biological context of Psmd1

• Molecular basis of reovirus virulence: role of the S1 gene [12].
• Primer extension and S1 nuclease analysis of RNA isolated from mouse stomachs aged between 2 and 25 days indicated that major transcription-initiation sites are between 22 and 25 base pairs 5' of the translation initiation site at all ages [13].
• However, the disappearance of S1 fibers was not related to these reduced activities, but to inhibited cell migration [14].
• S1 proteins on VFs, referred to here as S1 fibers, were lost in highly confluent cells, where cell proliferation and cellular metabolic activity greatly decreased owing to cell density-dependent arrest [14].
• Genetic studies indicate that the efficiency with which reovirus strains induce apoptosis is determined by the viral S1 gene, which encodes attachment protein sigma1 [15].

Anatomical context of Psmd1

• Thus, tolerance to PR8 S1 as a self peptide does not limit the diversity of the T cell response to S1(K113) [3].
• Using immunofluorescence techniques, monoclonal antibodies P140 and P112 , but not P256 , can be shown to bind to 80% of human monocytes [16].
• Interestingly, even though their numbers can vary, the S1-specific CD4+ CD25+ regulatory T cells in all cases coexist with clonally related CD4+ CD25- T cells that lack regulatory function [17].
• Biosynthesis of reovirus-specified polypeptides. Analysis of ribosome pausing during translation of reovirus S1 and S4 mRNAs in virus-infected and vector-transfected cells [18].
• S3 is situated within the stalk region that unfolds in response to mild acidification, and loads onto recycling H2-E(d) in the early endosome, while S1, located in the structurally constrained globular domain, loads onto nascent H2-E(d) in the late endosome [19].

Associations of Psmd1 with chemical compounds

• Previously, two rat monoclonal antibodies where developed which bind distinct epitopes on a murine glycoprotein, P112, which is expressed primarily in lung capillary endothelium [20].
• S1 proteins C2 and D2 are multifunctional hnRNP proteins acting as transcriptional regulators in the nucleus [14].
• In addition, alkylation of cysteine 41 of the S1 subunit, which may interact with NAD, inactivates the toxin but does not prevent binding by class A antibodies [21].
• The variants MM56, MM85, and MM78, selected by MAbs specific for the larger S protein of JHMV, were shown to have a deletion composed of about 150 aa located in the middle of the S1 subunit (MM56 and MM85) or one amino acid deletion, aspartic acid at number 543 from the N-terminus of the S1 (MM78) [22].
• In an effort to modulate S-1 and S-2 receptors in mouse brain, male C57BL/6J mice were treated chronically with methysergide, a serotonin antagonist with nanomolar affinity for both S-1 and S-2 receptors [23].

Analytical, diagnostic and therapeutic context of Psmd1

• The gene encoding the S1 subunit was subjected to site-specific mutagenesis in this critical region [1].
• Sequence analysis of S1(K113)-specific T cell receptors (TCR) from nontransgenic mice revealed a dominant TCR clonotype that cross-reacts with PR8 S1 [3].
• High levels of expression of recombinant S1 protein were observed in several transgenic lines by Western blot analysis using specific antibodies [5].
• Here, we verified the association of S1 proteins with vimentin using vimentin-deficient cells, crosslinking and immunoprecipitation, and further investigated the biological significance of this association [14].
• Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral cell attachment protein sigma 1 [24].

References