Unusual heterogeneity in the glycosylation of the G protein of the Hazelhurst strain of vesicular stomatitis virus

Hunt, Lawrence A.; Davidson, Sandra K.; Golemboski, Daniel

doi:10.1016/0003-9861(83)90301-6

Cited by 20 publications

(12 citation statements)

References 25 publications

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“…The G protein of the New Jersey serotype of VSV is known to contain some high-mannose type of oligosaccharide. 26) However, only one peak corresponding to the later peak of the control was detected in the case of the SS33410-treated cell fraction (Fig. 2B).…”

Section: Elution Proˆles Of Vsv G Glycopeptides Synthesized In the mentioning

confidence: 90%

SS33410, an Inhibitor of V-ATPase, Blocks Intracellular Protein Transport of the VSV-G Protein in the Golgi Compartment

Seog

2003

Bioscience, Biotechnology, and Biochemistry

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An earlier report suggested that SS33410, structurally related to folimycin and baˆlomycin A 1 , blocked secretion of the glycoprotein (G protein) of vesicular stomatitis virus (VSV) into the medium and, instead, G protein was accumulated intracellulary. To identify the inhibition site of SS33410 in intracellular protein transport, I have analyzed the oligosaccharide chain structure of the intracellularly accumulated G protein. In SS33410-treated VSV-infected cells, G protein oligosaccharide was suggested to have a composition of GlcNAc-Man 5 -GlcNAc 2 as analyzed by Bio-Gel P-4 column chromatography following digestion with a-mannosidase, b-N-acetylhexosaminidase, and then with a-mannosidase. SS33410 speciˆcally inhibited vacuolar-type ATPase (V-ATPase). These studies thus suggest that SS33410 blocks the intracellular protein transport before the step of trimming by mannosidase II, which is conˆned to the medial Golgi compartment.

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Section: Elution Proˆles Of Vsv G Glycopeptides Synthesized In the mentioning

confidence: 90%

SS33410, an Inhibitor of V-ATPase, Blocks Intracellular Protein Transport of the VSV-G Protein in the Golgi Compartment

Seog

2003

Bioscience, Biotechnology, and Biochemistry

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“…Compounds that block the Golgi dispersion induced by either BFA and nocodazole act on the centrosome and accelerate its microtubule-nucleating activity, while those that block only the before do not. 29) Golgi membrane dynamics are coordinated with cell-cycle progression and the Golgi is fragmented and dispersed at the onset of mitosis, [2][3][4][5] but subpopulations of Golgi proteins such as golgin-97 associate with the centrosome, even in the mitotic phase. 27) These centrosome-associated Golgi proteins might nucleate Golgi proteins into rebuilding the Golgi architecture after mitosis.…”

Section: Discussionmentioning

confidence: 99%

Mepanipyrim, a Novel Inhibitor of Pharmacologically Induced Golgi Dispersion

Nakamura¹,

Kono²,

Takatsuki³

2003

Bioscience, Biotechnology, and Biochemistry

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Mepanipyrim inhibited retrograde Golgi-to-ER trafficking induced by brefeldin A (BFA), nordihydroguaiaretic acid, clofibrate, and arachidonyltrifluoromethyl ketone in NRK and other types of cells, but did not inhibit anterograde trafficking of Golgi-resident proteins translocated to ER by BFA and newly synthesized VSV-G. However, mepanipyrim did not block the TGN38 dispersion induced by any of these compounds. Mepanipyrim acted on the Golgi, and swollen vesicular Golgi structures were formed and similar structures accumulated during rebuilding of the Golgi after BFA removal. These actions of mepanipyrim were readily reversed after its removal. Mepanipyrim did not stabilize microtubules, but prevented nocodazole-induced fragmentation and dispersion of the Golgi. These results suggest that the mepanipyrim-sensitive molecules participated in stabilizing the Golgi and its anchoring in the perinuclear region, and equally importantly, that the novel action of mepanipyrim may be used as a pharmacological tool for investigating membrane transport, Golgi membrane dynamics, and differentiation of the Golgi from TGN.

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“…One possibility is that the mature HN protein contains both high-mannose and complex oligosaccharides. The presence of both the 65,000-and 67,000-D species might represent incomplete endo H digestion, might mean that the 150min chase was insufficient to allow complete processing, or might mean that one site on the mature HN protein can contain either a high-mannose or a complex side chain, as has been described for other proteins (15,31). Nonetheless, these conditions were sufficient to document passage of HN through the Golgi complex.…”

Section: Maturation Of the Oligosaccharides In The Hn Proteinmentioning

confidence: 94%

Intracellular processing and transport of NH2-terminally truncated forms of a hemagglutinin-neuraminidase type II glycoprotein.

Spriggs

Collins

1990

The Journal of Cell Biology

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Abstract. Six amino-terminal deletion mutants of the NH2-terminally anchored (type II orientation) hemagglutinin-neuraminidase (HN) protein of parainfluenza virus type 3 were expressed in tissue culture by recombinant SV-40 viruses. The mutations consisted of progressive deletions of the cytoplasmic domain and, in some cases, of the hydrophobic signal/anchor. Three activities were dissociated for the signal/anchor: membrane insertion, translocation, and anchoring/transport. HN protein lacking the entire cytoplasmic tail was inserted efficiently into the membrane of the endoplasmic reticulum but was translocated inefficiently into the lumen. However, the small amounts that were successfully translocated appeared to be processed subsequently in a manner indistinguishable from that of parental HN. Thus, the cytoplasmic domain was not required for maturation of this type II glycoprotein. Progressive deletions into the membrane anchor restored efficient translocation, indicating that the NH2-terminal 44 amino acids were fully dispensable for membrane insertion and translocation and that a 10-amino acid hydrophobic signal sequence was sufficient for both activities. These latter HN molecules appeared to be folded authentically as assayed by hemagglutination activity, reactivity with a conformation-specific antiserum, correct formation of intramolecular disulfide bonds, and homooligomerization. However, most (85-90%) of these molecules accumulated in the ER. This showed that folding and oligomerization into a biologically active form, which presumably represents a virion spike, occurs essentially to completion within that compartment but is not sufficient for efficient transport through the exocytotic pathway. Protein transport also appeared to depend on the structure of the membrane anchor. These latter mutants were not stably integrated in the membrane, and the small proportion (10-15%) that was processed through the exocytotic pathway was secreted. The maturation steps and some of the effects of mutations described here for a type II glycoprotein resemble previous observations for prototypic type I glycoproteins and are indicative of close similarities in these processes for proteins of both membrane orientations.T H~ majority of integral membrane glycoproteins span the membrane once and are oriented with either their carboxy-terminal (type I) or amino-terminal (type II) amino acids exposed to the cytoplasm. Type I glycoproteins typically have a cleavable signal sequence at the amino terminus, a carboxy-proximal hydrophobic membrane anchor and a carboxy-terminal hydrophilic cytoplasmic tail. Type II glycoproteins are characterized by an amino-terminal cytoplasmic tail, followed by a 20-30-amino acid hydrophobic transmembrane domain, with the remainder of the protein being oriented externally, comprising the ectodomain.The intracellular processing and transport of membrane glycoproteins has been the object of extensive study. EluciDr. Spriggs's current address is lmmunex Corp., 51 University Street, Seattle WA 98101....

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Unusual heterogeneity in the glycosylation of the G protein of the Hazelhurst strain of vesicular stomatitis virus

Cited by 20 publications

References 25 publications

SS33410, an Inhibitor of V-ATPase, Blocks Intracellular Protein Transport of the VSV-G Protein in the Golgi Compartment

SS33410, an Inhibitor of V-ATPase, Blocks Intracellular Protein Transport of the VSV-G Protein in the Golgi Compartment

Mepanipyrim, a Novel Inhibitor of Pharmacologically Induced Golgi Dispersion

Intracellular processing and transport of NH2-terminally truncated forms of a hemagglutinin-neuraminidase type II glycoprotein.

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