Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum

Land, Aafke; Braakman, Ineke

doi:10.1016/s0300-9084(01)01314-1

Cited by 86 publications

(77 citation statements)

References 63 publications

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“…In vivo viral glycoproteins have been shown to influence infectivity (2), virulence (13), and host immune response (24,25). Added oligosaccharides confer proper function to viral glycoproteins since alteration of those glycosylation sites has shown dramatic consequences for viruses affecting protein folding (10,17,36) and protein active conformation (20). In this study, we analyzed the role of glycosylation of the CSFV E2 glycoprotein in virus virulence in swine.…”

Section: Discussionmentioning

confidence: 99%

N-Linked Glycosylation Status of Classical Swine Fever Virus Strain Brescia E2 Glycoprotein Influences Virulence in Swine

Risatti

Holinka

Sainz

et al. 2007

J Virol

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E2 is one of the three envelope glycoproteins of classical swine fever virus (CSFV). Previous studies indicate that E2 is involved in several functions, including virus attachment and entry to target cells, production of antibodies, induction of protective immune response in swine, and virulence. Here, we have investigated the role of E2 glycosylation of the highly virulent CSFV strain Brescia in infection of the natural host. Seven putative glycosylation sites in E2 were modified by site-directed mutagenesis of a CSFV Brescia infectious clone (BICv). A panel of virus mutants was obtained and used to investigate whether the removal of putative glycosylation sites in the E2 glycoprotein would affect viral virulence/pathogenesis in swine. We observed that rescue of viable virus was completely impaired by removal of all putative glycosylation sites in E2 but restored when mutation N185A reverted to wild-type asparagine produced viable virus that was attenuated in swine. Single mutations of each of the E2 glycosylation sites showed that amino acid N116 (N1v virus) was responsible for BICv attenuation. N1v efficiently protected swine from challenge with virulent BICv at 3 and 28 days postinfection, suggesting that glycosylation of E2 could be modified for development of classical swine fever live attenuated vaccines.

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Section: Discussionmentioning

confidence: 99%

N-Linked Glycosylation Status of Classical Swine Fever Virus Strain Brescia E2 Glycoprotein Influences Virulence in Swine

Risatti

Holinka

Sainz

et al. 2007

J Virol

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“…The attachment of sugar chains to proteins has been shown to inhibit selfassociation (Marquardt & Helenius, 1992;reviewed in Helenius et al, 1997;Land & Braakman, 2001;Song et al, 2001). This effect was largely attributed to covalently linked sugar moieties affecting kinetic partitioning between folding and aggregation from an (partially) unfolded state.…”

Section: Aggregation and Gelationmentioning

confidence: 99%

Application Potential of Food Protein Modification

Jongh¹,

Broersen²

2012

Advances in Chemical Engineering

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“…Alteration or abrogation of sites for glycosylation can have dramatic impact to survival and transmission of many viruses. Small alterations in glycosylation can alter folding and conformation that in turn affects the entire molecule [39][40][41]. Additionally, changes in the level of glycosylation can affect interaction with host receptors.…”

Section: Virus Glycosylationmentioning

confidence: 99%

Protein glycosylation in infectious disease pathobiology and treatment

Vigerust¹

2011

Open Life Sciences

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A host of bacteria and viruses are dependent on O-linked and N-linked glycosylation to perform vital biological functions. Pathogens often have integral proteins that participate in host-cell interactions such as receptor binding and fusion with host membrane. Fusion proteins from a broad range of disparate viruses, such as paramyxovirus, HIV, ebola, and the influenza viruses share a variety of common features that are augmented by glycosylation. Each of these viruses contain multiple glycosylation sites that must be processed and modified by the host post-translational machinery to be fusogenically active. In most viruses, glycosylation plays a role in biogenesis, stability, antigenicity and infectivity. In bacteria, glycosylation events play an important role in the formation of flagellin and pili and are vitally important to adherence, attachment, infectivity and immune evasion. With the importance of glycosylation to pathogen survival, it is clear that a better understanding of the processes is needed to understand the pathogen requirement for glycosylation and to capitalize on this requirement for the development of novel therapeutics.

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Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum

Cited by 86 publications

References 63 publications

N-Linked Glycosylation Status of Classical Swine Fever Virus Strain Brescia E2 Glycoprotein Influences Virulence in Swine

N-Linked Glycosylation Status of Classical Swine Fever Virus Strain Brescia E2 Glycoprotein Influences Virulence in Swine

Application Potential of Food Protein Modification

Protein glycosylation in infectious disease pathobiology and treatment

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