• Corpus ID: 51820143

[Frontiers in Bioscience 3, d354-364, March 22, 98] 354 BIOLOGY OF VACCINIA VIRUS ACYLPROTEINS

@inproceedings{Grosenbach1998FrontiersIB,
  title={[Frontiers in Bioscience 3, d354-364, March 22, 98] 354 BIOLOGY OF VACCINIA VIRUS ACYLPROTEINS},
  author={Douglas W. Grosenbach and Dennis E. Hruby},
  year={1998}
}
1. Abstract 2. Introduction 2.1 Overview of the vaccinia life cycle 2.2 Overview of protein fatty acylation 3. Identification of vaccinia acylproteins 3.1 Myristylproteins 3.2 Palmitylproteins 4. Biological significance of VV acylproteins 4.1 Myristylproteins 4.1.1 L1R 4.1.2 ATI 4.1.3 A14L 4.1.4 A16L, E7R, G9R 4.2 Palmitylproteins 4.2.1 p37 4.2.2 gp42 4.2.3 A33R 5. Perspective and future directions 5.1 Perspective 5.2 Future directions 5.2.1 Further analysis of VV myristylproteins 5.2.2 Further… 

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TLDR
Time course labeling of VV-infected cells with [3H]myristic acid reveals at least three additional putative myristylproteins, with apparent molecular masses of 92, 17, and 14 kDa, providing strong evidence that the open reading frames had been correctly identified and that each protein is my Bristylated on a glycine residue adjacent to the initiating methionine.
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Vaccinia virus-infected cells with [3H]myristic acid resulted in the incorporation of label into two viral proteins with apparent molecular weights of 35,000 and 25,000 (designated M35 and M25), suggesting greater stability of these proteins or a favored interaction of the proteins containing myristate with the maturing or intracellular virion.
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A detailed biochemical analysis of the major envelope antigen of vaccinia virus, M(r) 37,000 (p37K), showed that p37K is tightly bound to the viral envelope and resistance to proteinase K digestion indicates that it is not exposed on the surface of EEV but lines the inner side of the envelope.
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TLDR
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TLDR
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