Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The synthesis and organization of Sindbis virus structural proteins was investigated in BHK cells infected with wild-type virus (SVHR) or temperature-sensitive (ts) mutants defective in maturation. Cells infected with ts-23 or ts-20 (complementation groups D and E) were similar in the polypeptides synthesized at the nonpermissive temperature and differed from SVHR-infected cells in that the envelope protein E2 was not cleaved from the PE2 precursor. Data from experiments utilizing pulse-chase procedures or protein synthesis inhibitors indicated that although infectious virions were released from cells infected with these mutants in shift-down experiments, the particles were produced almost exclusively from proteins synthesized after the return to permissive temperature. This suggests that a stable complex may be formed among the structural proteins before budding. A membrane fraction isolated from cells infected with either ts mutants or SVHR contained the PE2, E1, and C polypeptides, whereas E2 was restricted to fractions obtained from SVHR-infected cells. Although equivalent amounts of virus-specific protein were synthesized in cells infected with either mutant and the cells contained qualitatively the same proteins in the isolated membranes, cells infected with ts-23 did not have virus-specific proteins exposed on their surface that could be detected by ferritin-conjugated antibody-labeling procedures or lactoperoxidase-mediated iodination. In contrast, ts-20-infected cells had significant amounts of viral protein, mainly E1, that could be detected on the plasma membrane by either procedure. Iodine was incorporated into E1 and E2 on the surface of SVHR-infected cells in the same relative amounts as seen in iodinated virions. PE2, however, although present in membranes, could not be iodinated on the surface of infected cells under any of the conditions used in this study. We also monitored the relative efficiency with which these viral proteins could be removed from intact cells by dilute solutions of nonionic detergents. The results indicated that E2 was most efficiently removed, followed by E1. PE2 (the precursor to E2) and C remained associated with the cell and could be subsequently isolated in the membrane fraction.
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PMID:Envelopments of Sindbis virus: synthesis and organization of proteins in cells infected with wild type and maturation-defective mutants. 87 34

Intact cells of Pseudomonas facilis contain one major molecular weight class of protein that is exposed at the cell surface as revealed by lactoperoxidase-catalyzed iodination with (125)I. All molecular weight classes of protein in derived cell envelope preparations are apparently saturated by iodination by lactoperoxidase after prolonged sonic treatment. The molecular weight of the predominantly exposed protein in intact cells is approximately 16,000, which is the minimal molecular weight of a cell envelope protein that precipitates as a complex with phospholipid from extracts of P. facilis. The isolation of labeled phospholipoprotein (PLP) after labeling intact cells with (125)I corroborates previous experiments which suggested a surface location for the protein portion of the phospholipoprotein (P(PLP)). Solvent extraction of cells and immunological evidence, including studies with ferritin-coupled antibodies, indicate that P(PLP) is located at the cell surface and may also be within the cell envelope. These experiments suggest that P(PLP) is the major cell surface protein in P. facilis.
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PMID:Cell surface protein of Pseudomonas (Hydrogenomonas) facilis. 419 5

A protein with a molecular weight of 60,000 (60K) constitutes approximately 20% of the envelope protein of Azotobacter vinelandii. This protein was removed from cells and purified from other proteins by a simple washing procedure that had no effect on cell viability. Anti-60K antiserum blocked azotophage A-22 adsorption and agglutinated both vegetative cells and cysts; ferritin-conjugated antibodies used in indirect labeling studies bound uniformly to the periphery of vegetative cells. We conclude that 60K is present on the outer surface of vegetative cells and cysts. The protein is similar to the surface protein alpha of Acinetobacter ssp. in molecular weight, reassociation characteristics, and high ratio of acidic to basic amino acids. We propose that 60K forms a layer external to the outer membrane of A. vinelandii.
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PMID:Characterization of the predominant Azotobacter vinelandii envelope protein. 678 19

It is well known that iron is an essential element for all living organism. The intracellular iron availability is also important for the host's innate immune response to various pathogens, in which the iron homeostasis can be regulated by ferritin due to its iron storage property. In this study, a full-length cDNA sequence of ferritin (named as CqFerritin) was identified with 1410 bp from red claw crayfish Cherax quadricarinatus, which contained an open reading frame of 513 bp, encoding 170 amino acids with a conserved ferritin domain. Tissue distribution analysis demonstrated that CqFerritin was widely expressed in various tissues with high presence in haemocyte, haematopoietic tissue (Hpt) and heart, while lowest expression in hepatopancreas. In addition, loss-of-function of CqFerritin by gene silencing resulted in significantly higher expression of an envelope protein VP28 of white spot syndrome virus (WSSV) in red claw crayfish Hpt cell cultures, indicating the potential antiviral response of CqFerritin. To further explore the effect on WSSV replication by CqFerritin, recombinant CqFerritin protein (rCqFerritin) was transfected into Hpt cells followed by WSSV infection. Importantly, the replication of WSSV was obviously decreased in Hpt cells if transfected with rCqFerritin protein, suggesting that CqFerritin had clearly negative effect on WSSV infection. Furthermore, intracellular accumulation of iron ions was found to promote the WSSV replication in a dose-dependent manner, illustrating that the iron level regulated by CqFerritin was likely to be vital for WSSV infection in red claw crayfish. Taken together, these data suggest that CqFerritin plays an important role in immune defense against WSSV infection in a crustacean C. quadricarinatus.
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PMID:A CqFerritin protein inhibits white spot syndrome virus infection via regulating iron ions in red claw crayfish Cherax quadricarinatus. 2934 72