Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells

Berlo, M. F. van; Brink, W van den; Horzinek, Marian C.; Zeijst, Bernard A.M. van der

doi:10.1007/bf01311339

Cited by 25 publications

(19 citation statements)

References 21 publications

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“…On the carboxy-terminal side, the membrane anchor region is flanked by an unusually high number of cysteine residues. This feature has also been recognized in other coronavirus S proteins (Rasschaert & Laude, 1987;Schmidt et al, 1987) and it has been proposed that at least some of these residues may be involved in the acylation of the S protein which has been described for MHV , van Berlo et al, 1987. In the HCV 229E S protein sequence it is also possible to identify the 'heptad repeat' structures (corresponding to amino acids 794 to 849, Fig.…”

Section: Sequence Analysis Of the Hcv 229e S Protein Genementioning

confidence: 73%

Nucleotide Sequence of the Gene Encoding the Spike Glycoprotein of Human Coronavirus HCV 229E

Raabe

Schelle-Prinz

Siddell

1990

Journal of General Virology

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The gene encoding the spike glycoprotein of the human coronavirus HCV 229E has been cloned and sequenced. This analysis predicts an S polypeptide of 1173 amino acids with an M, of 128600. The polypeptide has 30 potential N-glycosylation sites. A number of structural features typical of coronavirus S proteins can be recognized, including a signal sequence, a membrane anchor, heptad repeat structures and a carboxy-terminal cysteine cluster. A detailed, computer-aided comparison with the S proteins of infectious bronchitis virus, feline infectious peritonitis virus, transmissible gastroenteritis virus and murine hepatitis virus, strain JHM is presented. We have also done a Northern blot analysis of viral RNAs in HCV 229E-infected cells using synthetic oligonucleotides. On the basis of this analysis, and by analogy to the replication strategy of other coronaviruses, we are able to propose a model for the organization and expression of the HCV 229E genome.

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Section: Sequence Analysis Of the Hcv 229e S Protein Genementioning

confidence: 73%

Nucleotide Sequence of the Gene Encoding the Spike Glycoprotein of Human Coronavirus HCV 229E

Raabe

Schelle-Prinz

Siddell

1990

Journal of General Virology

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“…One role for cysteine residues in this region of the spike is to serve as sites for the covalent attachment of palmitic acid (Ponimaskin and Schmidt, 1995;Rose et al, 1984;Schlesinger et al, 1993;Schmidt, 1989;Sefton and Buss, 1987). The spike protein is palmitylated on the carboxyl-terminal S2 fragment (Niemann and Klenk, 1981;Schmidt, 1982;Sturman et al, 1985;van Berlo et al, 1987). Palmitate is generally attached to viral fusion proteins through a thioester bond involving cysteines that reside near the inner leaflet of the plasma membrane (Ponimaskin and Schmidt, 1995;Rose et al, 1984;Schlesinger et al, 1993;Schmidt, 1989;Sefton and Buss, 1987).…”

Section: Discussionmentioning

confidence: 99%

Coronavirus-Induced Membrane Fusion Requires the Cysteine-Rich Domain in the Spike Protein

2000

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The spike glycoprotein of mouse hepatitis virus strain A59 mediates the early events leading to infection of cells, including fusion of the viral and cellular membranes. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail. In this study, we examined the role of these carboxyl-terminal domains in spike-mediated membrane fusion. We show that the cytoplasmic tail is not required for fusion but has the capacity to enhance membrane fusion activity. Chimeric spike protein mutants containing substitutions of the entire transmembrane anchor and cys domain with the herpes simplex virus type 1 glycoprotein D (gD-1) anchor demonstrated that fusion activity requires the presence of the A59 membrane-spanning domain and the portion of the cys domain that lies upstream of the cytoplasmic tail. The cys domain is a required element since its deletion from the wild-type spike protein abrogates fusion activity. However, addition of the cys domain to fusion-defective chimeric proteins was unable to restore fusion activity. Thus, the cys domain is necessary but is not sufficient to complement the gD-1 anchor and allow for membrane fusion. Site-specific mutations of conserved cysteine residues in the cys domain markedly reduce membrane fusion, which further supports the conclusion that this region is crucial for spike function. The results indicate that the carboxyl-terminus of the spike transmembrane anchor contains at least two distinct domains, both of which are necessary for full membrane fusion.

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“…The N-linked sugars are modified and become mature during passage through the Golgi complex. The MHV S protein was shown to become palmitoylated, a modification that may already take place in the endoplasmic reticulum (van Berlo et al, 1987). As a late step the S protein can be cleaved.…”

Section: F S Proteinmentioning

confidence: 99%