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Thematische Bibliographien / Glycoproteins / Zeitschriftenartikel

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Zeitschriftenartikel zum Thema „Glycoproteins“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 25. Juli 2025

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1

Garbutt, Michael, Ryan Liebscher, Victoria Wahl-Jensen, et al. "Properties of Replication-Competent Vesicular Stomatitis Virus Vectors Expressing Glycoproteins of Filoviruses and Arenaviruses." Journal of Virology 78, no. 10 (2004): 5458–65. http://dx.doi.org/10.1128/jvi.78.10.5458-5465.2004.

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ABSTRACT Replication-competent recombinant vesicular stomatitis viruses (rVSVs) expressing the type I transmembrane glycoproteins and selected soluble glycoproteins of several viral hemorrhagic fever agents (Marburg virus, Ebola virus, and Lassa virus) were generated and characterized. All recombinant viruses exhibited rhabdovirus morphology and replicated cytolytically in tissue culture. Unlike the rVSVs with an additional transcription unit expressing the soluble glycoproteins, the viruses carrying the foreign transmembrane glycoproteins in replacement of the VSV glycoprotein were slightly a

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Jorgenson, Rebecca L., Volker M. Vogt, and Marc C. Johnson. "Foreign Glycoproteins Can Be Actively Recruited to Virus Assembly Sites during Pseudotyping." Journal of Virology 83, no. 9 (2009): 4060–67. http://dx.doi.org/10.1128/jvi.02425-08.

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ABSTRACT Retroviruses like human immunodeficiency virus type 1 (HIV-1), as well as many other enveloped viruses, can efficiently produce infectious virus in the absence of their own surface glycoprotein if a suitable glycoprotein from a foreign virus is expressed in the same cell. This process of complementation, known as pseudotyping, often can occur even when the glycoprotein is from an unrelated virus. Although pseudotyping is widely used for engineering chimeric viruses, it has remained unknown whether a virus can actively recruit foreign glycoproteins to budding sites or, alternatively, i

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Quinn, Derek J., Neil V. McFerran, John Nelson, and W. Paul Duprex. "Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology." Bioscience Reports 32, no. 3 (2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.

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Protein interactions play key roles throughout all subcellular compartments. In the present paper, we report the visualization of protein interactions throughout living mammalian cells using two oligomerizing MV (measles virus) transmembrane glycoproteins, the H (haemagglutinin) and the F (fusion) glycoproteins, which mediate MV entry into permissive cells. BiFC (bimolecular fluorescence complementation) has been used to examine the dimerization of these viral glycoproteins. The H glycoprotein is a type II membrane-receptor-binding homodimeric glycoprotein and the F glycoprotein is a type I di

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Lay Mendoza, Maria Fernanda, Marissa Danielle Acciani, Courtney Nina Levit, Christopher Santa Maria, and Melinda Ann Brindley. "Monitoring Viral Entry in Real-Time Using a Luciferase Recombinant Vesicular Stomatitis Virus Producing SARS-CoV-2, EBOV, LASV, CHIKV, and VSV Glycoproteins." Viruses 12, no. 12 (2020): 1457. http://dx.doi.org/10.3390/v12121457.

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Viral entry is the first stage in the virus replication cycle and, for enveloped viruses, is mediated by virally encoded glycoproteins. Viral glycoproteins have different receptor affinities and triggering mechanisms. We employed vesicular stomatitis virus (VSV), a BSL-2 enveloped virus that can incorporate non-native glycoproteins, to examine the entry efficiencies of diverse viral glycoproteins. To compare the glycoprotein-mediated entry efficiencies of VSV glycoprotein (G), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S), Ebola (EBOV) glycoprotein (GP), Lassa (LASV) G

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Joshua, G. W. P., L. J. S. Harrison, and M. M. H. Sewell. "Developmental changes in proteins and glycoproteins revealed by direct radio-iodination of viable Taenia saginata larvae." Parasitology 99, no. 2 (1989): 265–74. http://dx.doi.org/10.1017/s0031182000058728.

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SummaryDirect surface I radio-isotope labelling techniques and SDS—PAGE analysis were used to compare the proteins and lentil—lectin adherent glycoproteins of the bovine stage of viable Taenia saginata larvae at three points in their development, the invasive oncospheres, immature (4-week-old) and mature (12 to 16-week-old) cysticerci. Some proteins and glycoproteins were present on all three of the ages of the parasite examined but there were also distinct age-specific proteins and glycoproteins detected on oncospheres and 4-week-old cysticerci and a marked difference between the protein/glyc

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Zhang, Libo, Yanhong Li, Riyao Li, et al. "Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed in E. coli." Molecules 28, no. 6 (2023): 2753. http://dx.doi.org/10.3390/molecules28062753.

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Protein N-glycosylation is a common post-translational modification that plays significant roles on the structure, property, and function of glycoproteins. Due to N-glycan heterogeneity of naturally occurring glycoproteins, the functions of specific N-glycans on a particular glycoprotein are not always clear. Glycoprotein in vitro N-glycan engineering using purified recombinant enzymes is an attractive strategy to produce glycoproteins with homogeneous N-glycoforms to elucidate the specific functions of N-glycans and develop better glycoprotein therapeutics. Toward this goal, we have successfu

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Si, Zhihai, Mark Cayabyab, and Joseph Sodroski. "Envelope Glycoprotein Determinants of Neutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys." Journal of Virology 75, no. 9 (2001): 4208–18. http://dx.doi.org/10.1128/jvi.75.9.4208-4218.2001.

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ABSTRACT The simian-human immunodeficiency virus SHIV-HXBc2 contains the envelope glycoproteins of a laboratory-adapted, neutralization-sensitive human immunodeficiency virus type 1 variant, HXBc2. Serial in vivo passage of the nonpathogenic SHIV-HXBc2 generated SHIV KU-1, which causes rapid CD4+ T-cell depletion and an AIDS-like illness in monkeys. A molecularly cloned pathogenic SHIV, SHIV-HXBc2P 3.2, was derived from the SHIV KU-1 isolate and differs from the parental SHIV-HXBc2 by only 12 envelope glycoprotein amino acid residues. Relative to SHIV-HXBc2, SHIV-HXBc2P 3.2 was resistant to ne

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Calvete, J. J., J. L. McGregor, G. Rivas, and J. González-Rodríguez. "Identification of a Glycoprotein III a Dimer in Polyacrylamide Gel Separations of Human Platelet Membranes." Thrombosis and Haemostasis 58, no. 02 (1987): 694–97. http://dx.doi.org/10.1055/s-0038-1645957.

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SummaryMembrane glycoproteins IIb and IIIa play a major role in human blood platelet aggregation. The absence or the severe reduction of these two membrane glycoproteins, as observed in platelets of Glanzmann’s thrombasthenic patients, is related to a lack of platelet aggregation. Separation of Glanzmann’s thrombasthenic platelet samples by two-dimensional polyacrylamide O’Farrell gels show the absence of a high and several low molecular mass glycoproteins, in addition to the loss of glycoproteins IIb and IIIa (McGregor J. L. et al. Eur. J. Biochem. 1981; 116: 379-388). The aim of this study w

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LaBonte, Jason A., Navid Madani, and Joseph Sodroski. "Cytolysis by CCR5-Using Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Is Dependent on Membrane Fusion and Can Be Inhibited by High Levels of CD4 Expression." Journal of Virology 77, no. 12 (2003): 6645–59. http://dx.doi.org/10.1128/jvi.77.12.6645-6659.2003.

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ABSTRACT T-tropic (X4) and dualtropic (R5X4) human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins kill primary and immortalized CD4+ CXCR4+ T cells by mechanisms involving membrane fusion. However, because much of HIV-1 infection in vivo is mediated by M-tropic (R5) viruses whose envelope glycoproteins use CCR5 as a coreceptor, we tested a panel of R5 and R5X4 envelope glycoproteins for their ability to lyse CCR5+ target cells. As is the case for CXCR4+ target cells, HIV-1 envelope glycoproteins expressed by single-round HIV-1 vectors killed transduced CD4+ CCR5+ cells in a membr

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Shammala, Farid Abu. "Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery." Brazilian Journal of Biological Sciences 4, no. 7 (2017): 203–15. http://dx.doi.org/10.21472/bjbs.040720.

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Most proteins are glycosylated, glycosylation is one of the most important posttranslational modifications of proteins and plays essential roles in various biological processes. Aberration in the glycan moieties of glycoproteins is associated with many diseases. It is especially critical to develop the rapid and sensitive methods for analysis of aberrant glycoproteins associated with diseases. With recent advances in proteomics, analytical and computational technologies, glycoproteomics, the global analysis of glycoproteins, is rapidly emerging as a subfield of proteomics with high biological

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Yang, Xinzhen, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt, and Joseph Sodroski. "Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin." Journal of Virology 76, no. 9 (2002): 4634–42. http://dx.doi.org/10.1128/jvi.76.9.4634-4642.2002.

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ABSTRACT The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a trimer composed of three gp120 exterior glycoproteins and three gp41 transmembrane proteins. Soluble gp140 glycoproteins composed of the uncleaved ectodomains of gp120 and gp41 form unstable, heterogeneous oligomers, but soluble gp140 trimers can be stabilized by fusion with a C-terminal, trimeric GCN4 motif (X. Yang et al., J. Virol. 74:5716-5725, 2000). To understand the influence of the C-terminal trimerization domain on the properties of soluble HIV-1 envelope glycoprotein trimers, uncleaved, s

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Ji, Xin, Gene G. Olinger, Sheena Aris, Ying Chen, Henry Gewurz, and Gregory T. Spear. "Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization." Journal of General Virology 86, no. 9 (2005): 2535–42. http://dx.doi.org/10.1099/vir.0.81199-0.

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Mannose-binding lectin (MBL), a serum lectin that mediates innate immune functions including activation of the lectin complement pathway, binds to carbohydrates expressed on some viral glycoproteins. In this study, the ability of MBL to bind to virus particles pseudotyped with Ebola and Marburg envelope glycoproteins was evaluated. Virus particles bearing either Ebola (Zaire strain) or Marburg (Musoke strain) envelope glycoproteins bound at significantly higher levels to immobilized MBL compared with virus particles pseudotyped with vesicular stomatitis virus glycoprotein or with no virus glyc

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Ninagawa, Satoshi, Tetsuya Okada, Yoshiki Sumitomo, et al. "Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway." Journal of Cell Biology 211, no. 4 (2015): 775–84. http://dx.doi.org/10.1083/jcb.201504109.

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Glycoproteins and non-glycoproteins possessing unfolded/misfolded parts in their luminal regions are cleared from the endoplasmic reticulum (ER) by ER-associated degradation (ERAD)-L with distinct mechanisms. Two-step mannose trimming from Man9GlcNAc2 is crucial in the ERAD-L of glycoproteins. We recently showed that this process is initiated by EDEM2 and completed by EDEM3/EDEM1. Here, we constructed chicken and human cells simultaneously deficient in EDEM1/2/3 and analyzed the fates of four ERAD-L substrates containing three potential N-glycosylation sites. We found that native but unstable

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Choukhi, Amélie, André Pillez, Hervé Drobecq, Christian Sergheraert, Czeslaw Wychowski, and Jean Dubuisson. "Characterization of aggregates of hepatitis C virus glycoproteins." Journal of General Virology 80, no. 12 (1999): 3099–107. http://dx.doi.org/10.1099/0022-1317-80-12-3099.

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Hepatitis C virus (HCV) encodes two glycoproteins, E1 and E2, which assemble in oligomeric structures. Studies of HCV glycoprotein assembly using heterologous expression systems have shown that these glycoproteins can follow two pathways: a productive pathway leading to the formation of a non-covalent heterodimer; and a non-productive pathway leading to the formation of large disulfide-linked aggregates. The non-covalent HCV glycoprotein complex is probably the functional complex which plays an active role in the entry process in host cells. The aggregates are believed to be waste products; ho

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Snyder, Aleksandra, Todd W. Wisner, and David C. Johnson. "Herpes Simplex Virus Capsids Are Transported in Neuronal Axons without an Envelope Containing the Viral Glycoproteins." Journal of Virology 80, no. 22 (2006): 11165–77. http://dx.doi.org/10.1128/jvi.01107-06.

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ABSTRACT Electron micrographic studies of neuronal axons have produced contradictory conclusions on how alphaherpesviruses are transported from neuron cell bodies to axon termini. Some reports have described unenveloped capsids transported on axonal microtubules with separate transport of viral glycoproteins within membrane vesicles. Others have observed enveloped virions in proximal and distal axons. We characterized transport of herpes simplex virus (HSV) in human and rat neurons by staining permeabilized neurons with capsid- and glycoprotein-specific antibodies. Deconvolution microscopy was

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Sandrin, Virginie, Delphine Muriaux, Jean-Luc Darlix, and François-Loïc Cosset. "Intracellular Trafficking of Gag and Env Proteins and Their Interactions Modulate Pseudotyping of Retroviruses." Journal of Virology 78, no. 13 (2004): 7153–64. http://dx.doi.org/10.1128/jvi.78.13.7153-7164.2004.

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ABSTRACT Glycoproteins derived from most retroviruses and from several families of enveloped viruses can form infectious pseudotypes with murine leukemia virus (MLV) and lentiviral core particles, like the MLV envelope glycoproteins (Env) that are incorporated on either virus type. However, coexpression of a given glycoprotein with heterologous core proteins does not always give rise to highly infectious viral particles, and restrictions on pseudotype formation have been reported. To understand the mechanisms that control the recruitment of viral surface glycoproteins on lentiviral and retrovi

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Yang, Xinzhen, Svetla Kurteva, Xinping Ren, Sandra Lee, and Joseph Sodroski. "Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells." Journal of Virology 80, no. 9 (2006): 4388–95. http://dx.doi.org/10.1128/jvi.80.9.4388-4395.2006.

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ABSTRACT The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a homotrimer of gp120/gp41 heterodimers to support virus entry. During the process of virus entry, an individual HIV-1 envelope glycoprotein trimer binds the cellular receptors CD4 and CCR5/CXCR4 and mediates the fusion of the viral and the target cellular membranes. By studying the function of heterotrimers between wild-type and nonfunctional mutant envelope glycoproteins, we found that two wild-type subunits within an envelope glycoprotein trimer are required to support virus entry. Complementation

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Rosenberg, Arielle R., Lélia Delamarre, Anna Preira, and Marie-Christine Dokhélar. "Analysis of Functional Conservation in the Surface and Transmembrane Glycoprotein Subunits of Human T-Cell Leukemia Virus Type 1 (HTLV-1) and HTLV-2." Journal of Virology 72, no. 9 (1998): 7609–14. http://dx.doi.org/10.1128/jvi.72.9.7609-7614.1998.

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ABSTRACT Human T-cell leukemia virus types 1 and 2 (HTLV-1 and HTLV-2) are closely related retroviruses with nucleotide sequences that are 65% identical. To determine whether their envelope glycoproteins function similarly and to define the molecular determinants of HTLV-2 envelope-mediated functions, we have used pseudotyped viruses and have introduced mutations into regions of the HTLV-2 glycoproteins homologous to those known to be important for HTLV-1 glycoprotein functions. The envelopes of the two viruses could be exchanged with no loss of infectivity, suggesting that the glycoproteins f

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Karger, Axel, Ulrike Schmidt, and Ursula J. Buchholz. "Recombinant bovine respiratory syncytial virus with deletions of the G or SH genes: G and F proteins bind heparin." Journal of General Virology 82, no. 3 (2001): 631–40. http://dx.doi.org/10.1099/0022-1317-82-3-631.

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Bovine respiratory syncytial virus (BRSV) encodes three transmembrane envelope glycoproteins, namely the small hydrophobic (SH) protein, the attachment glycoprotein (G) and the fusion glycoprotein (F). The BRSV reverse genetics system has been used to generate viable recombinant BRSV lacking either the G gene or the SH gene or both genes. The deletion mutants were fully competent for multicycle growth in cell culture, proving that, of the BRSV glycoprotein genes, the SH and G genes are non-essential. Virus morphogenesis was not impaired by either of the deletions. The deletion mutants were use

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Børsum, Tone. "Immunoelectrophoretic Analysis of Membrane Glycoproteins in Cultured Human Endothelial Cells." Thrombosis and Haemostasis 63, no. 02 (1990): 303–11. http://dx.doi.org/10.1055/s-0038-1645214.

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SummaryHuman endothelial cells isolated from umbilical cordswere solubilized in Triton X-100 and examined by crossedimmunoelec-trophoresis using rabbit antiserum against endothelial cells. Endogenous labelling of the endothelialcell proteins with 14Cmannose followed by crossed immunoelectrophoresis and autoradiography revealed about 10 immunoprecipitates. Four of these endothelial cell glycoproteins were labelled by lactoperoxidase catalyzed iodination and thus were surface located. Three of the surface located glycoproteins showed reduced electrophoretic mobility after incubation of the endot

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Bloodgood, R. A., and N. L. Salomonsky. "The transmembrane signaling pathway involved in directed movements of Chlamydomonas flagellar membrane glycoproteins involves the dephosphorylation of a 60-kD phosphoprotein that binds to the major flagellar membrane glycoprotein." Journal of Cell Biology 127, no. 3 (1994): 803–11. http://dx.doi.org/10.1083/jcb.127.3.803.

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Cross-linking of Chlamydomonas reinhardtii flagellar membrane glycoproteins results in the directed movements of these glycoproteins within the plane of the flagellar membrane. Three carbohydrate-binding reagents (FMG-1 monoclonal antibody, FMG-3 monoclonal antibody, concanvalin A) that induce flagellar membrane glycoprotein crosslinking and redistribution also induce the specific dephosphorylation of a 60-kD (pI 4.8-5.0) flagellar phosphoprotein (pp60) that is phosphorylated in vivo on serine. Ethanol treatment of live cells induces a similar specific dephosphorylation of pp60. Affinity adsor

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Weaver, T. E., J. A. Whitsett, W. M. Hull, and G. Ross. "Identification of canine pulmonary surfactant-associated glycoprotein A precursors." Journal of Applied Physiology 58, no. 6 (1985): 2091–95. http://dx.doi.org/10.1152/jappl.1985.58.6.2091.

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Surfactant-associated glycoproteins A were identified by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis of crude surfactant from canine alveolar lavage: an unglycosylated form (protein A1), 27,000–28,000 daltons; glycoprotein A2, 32,000–34,000 daltons; and glycoprotein A3, 37,000–38,000 daltons; pH at isoelectric point (pI) 4.5–5.0. Glycoproteins A2 and A3 were electroeluted and used to prepare a monospecific antiserum that identified proteins A1, A2, and A3 in immunoblots of crude surfactant obtained from dog lung lavage. This antiserum precipitated several proteins

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Batonick, Melissa, and Gail W. Wertz. "Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells." Advances in Virology 2011 (2011): 1–11. http://dx.doi.org/10.1155/2011/343408.

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Human respiratory syncytial virus (HRSV) is an enveloped RNA virus that assembles and buds from the plasma membrane of infected cells. The ribonucleoprotein complex (RNP) must associate with the viral matrix protein and glycoproteins to form newly infectious particles prior to budding. The viral proteins involved in HRSV assembly and egress are mostly unexplored. We investigated whether the glycoproteins of HRSV were involved in the late stages of viral replication by utilizing recombinant viruses where each individual glycoprotein gene was deleted and replaced with a reporter gene to maintain

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Bieńkowska-Szewczyk, K., and B. Szewczyk. "Expression of genes coding for animal virus glycoproteins in heterologous systems." Acta Biochimica Polonica 46, no. 2 (1999): 325–39. http://dx.doi.org/10.18388/abp.1999_4166.

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The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expr

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Kukushkin, Nikolay V., Dominic S. Alonzi, Raymond A. Dwek, and Terry D. Butters. "Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase." Biochemical Journal 438, no. 1 (2011): 133–42. http://dx.doi.org/10.1042/bj20110186.

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During quality control in the ER (endoplasmic reticulum), nascent glycoproteins are deglucosylated by ER glucosidases I and II. In the post-ER compartments, glycoprotein endo-α-mannosidase provides an alternative route for deglucosylation. Previous evidence suggests that endomannosidase non-selectively deglucosylates glycoproteins that escape quality control in the ER, facilitating secretion of aberrantly folded as well as normal glycoproteins. In the present study, we employed FOS (free oligosaccharides) released from degrading glycoproteins as biomarkers of ERAD (ER-associated degradation),

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Lisanti, M. P., A. Le Bivic, M. Sargiacomo, and E. Rodriguez-Boulan. "Steady-state distribution and biogenesis of endogenous Madin-Darby canine kidney glycoproteins: evidence for intracellular sorting and polarized cell surface delivery." Journal of Cell Biology 109, no. 5 (1989): 2117–27. http://dx.doi.org/10.1083/jcb.109.5.2117.

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We used domain-selective biotinylation/125I-streptavidin blotting (Sargiacomo, M., M. P. Lisanti, L. Graeve, A. Le Bivic, and E. Rodriguez-Boulan. 1989 J. Membr. Biol. 107:277-286), in combination with lectin precipitation, to analyze the apical and basolateral glycoprotein composition of Madin-Darby canine kidney (MDCK) cells and to explore the role of glycosylation in the targeting of membrane glycoproteins. All six lectins used recognized both apical and basolateral glycoproteins, indicating that none of the sugar moieties detected were characteristic of the particular epithelial cell surfa

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Bude, Sara Amanuel, Zengjun Lu, Zhixun Zhao, and Qiang Zhang. "Pseudorabies Virus Glycoproteins E and B Application in Vaccine and Diagnosis Kit Development." Vaccines 12, no. 9 (2024): 1078. http://dx.doi.org/10.3390/vaccines12091078.

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Background: Pseudorabies virus (PRV) is a highly infectious pathogen that affects a wide range of mammals and imposes a significant economic burden on the global pig industry. The viral envelope of PRV contains several glycoproteins, including glycoprotein E (gE) and glycoprotein B (gB), which play critical roles in immune recognition, vaccine development, and diagnostic procedures. Mutations in these glycoproteins may enhance virulence, highlighting the need for updated vaccines. Method: This review examines the functions of PRV gE and gB in vaccine development and diagnostics, focusing on th

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Hulswit, Ruben J. G., Guido C. Paesen, Thomas A. Bowden, and Xiaohong Shi. "Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure." Viruses 13, no. 2 (2021): 353. http://dx.doi.org/10.3390/v13020353.

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The Bunyavirales order accommodates related viruses (bunyaviruses) with segmented, linear, single-stranded, negative- or ambi-sense RNA genomes. Their glycoproteins form capsomeric projections or spikes on the virion surface and play a crucial role in virus entry, assembly, morphogenesis. Bunyavirus glycoproteins are encoded by a single RNA segment as a polyprotein precursor that is co- and post-translationally cleaved by host cell enzymes to yield two mature glycoproteins, Gn and Gc (or GP1 and GP2 in arenaviruses). These glycoproteins undergo extensive N-linked glycosylation and despite thei

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Bloodgood, R. A., and N. L. Salomonsky. "Calcium influx regulates antibody-induced glycoprotein movements within the Chlamydomonas flagellar membrane." Journal of Cell Science 96, no. 1 (1990): 27–33. http://dx.doi.org/10.1242/jcs.96.1.27.

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The Chlamydomonas flagellar surface exhibits a number of dynamic membrane phenomena associated with whole-cell gliding locomotion and the early events in fertilization. Crosslinking of a specific population of flagellar surface-exposed glycoproteins with the lectin concanavalin A or an anti-carbohydrate mouse monoclonal antibody, designated FMG-1, results in a characteristic pattern of glycoprotein redistribution within the plane of the flagellar membrane. Recent evidence suggests that flagellar membrane glycoprotein movements are associated with both whole-cell gliding motility and the early

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Horvat, B., H. A. Multhaupt, and I. Damjanov. "Glycoproteins of mouse vaginal epithelium: differential expression related to estrous cyclicity." Journal of Histochemistry & Cytochemistry 41, no. 9 (1993): 1351–57. http://dx.doi.org/10.1177/41.9.8354876.

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We used lectin overlay blotting and SDS-PAGE to analyze the estrous cycle-specific expression of mouse vaginal epithelial glycoproteins. Seven lectins chosen for their differential carbohydrate-binding specificity revealed 15 glycoproteins that showed cycle-related expression. Each lectin had a unique binding pattern different from the patterns revealed by other lectins. However, several estrous cycle phase-specific glycoproteins reacted with more than one lectin. The most prominent of these glycoproteins (M(r) 92-95 KD) was weakly expressed in late diestrus and fully expressed only in proestr

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Srivastav, Archana, Balvir Singh, Abhishek Chandra, Farrukh Jamal, Mohammad Y. Khan, and Sunil R. Chowdhury. "Partial characterization, sperm association and significance of N- and O-linked glycoproteins in epididymal fluid of rhesus monkeys (Macaca mulatta)." Reproduction 127, no. 3 (2004): 343–57. http://dx.doi.org/10.1530/rep.1.00119.

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The present study investigated regional modifications of glycosylation status, sperm association and functional significance of N- and O-linked glycoproteins in epididymal luminal fluid of the rhesus monkey (Macaca mulatta). The predominant glycoproteins of the epididymal luminal fluid that increase in the extent of glycosylation or unmasking of exposed epitopes in a region-specific, maturation-dependent manner, included those of 150, 116, 68, 64, 58 (N- and O-linked) and 170 kDa (O-linked). The higher expression of 40 (N-linked), 38 (N- and O-linked) and 60, 56 and 33 kDa (O-linked) glycoprot

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Zimmer, Gert, Klaus-Peter Zimmer, Ina Trotz, and Georg Herrler. "Vesicular Stomatitis Virus Glycoprotein Does Not Determine the Site of Virus Release in Polarized Epithelial Cells." Journal of Virology 76, no. 8 (2002): 4103–7. http://dx.doi.org/10.1128/jvi.76.8.4103-4107.2002.

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ABSTRACT In polarized epithelial cells, the vesicular stomatitis virus glycoprotein is segregated to the basolateral plasma membrane, where budding of the virus takes place. We have generated recombinant viruses expressing mutant glycoproteins without the basolateral-membrane-targeting signal in the cytoplasmic domain. Though about 50% of the mutant glycoproteins were found at the apical plasma membranes of infected MDCK cells, the virus was still predominantly released at the basolateral membranes, indicating that factors other than the glycoprotein determine the site of virus budding.

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Vollenweider, Florence, Felix Kappeler, Christian Itin, and Hans-Peter Hauri. "Mistargeting of the Lectin ERGIC-53 to the Endoplasmic Reticulum of HeLa Cells Impairs the Secretion of a Lysosomal Enzyme." Journal of Cell Biology 142, no. 2 (1998): 377–89. http://dx.doi.org/10.1083/jcb.142.2.377.

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ERGIC-53, a homo-oligomeric recycling protein associated with the ER–Golgi intermediate compartment (ERGIC), has properties of a mannose-selective lectin in vitro, suggesting that it may function as a transport receptor for glycoproteins in the early secretory pathway. To investigate if ERGIC-53 is involved in glycoprotein secretion, a mutant form of this protein was generated that is incapable of leaving the ER. If expressed in HeLa cells in a tetracycline-inducible manner, this mutant accumulated in the ER and retained the endogenous ERGIC-53 in this compartment, thus preventing its recyclin

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Rosenberg, Arielle R., Lélia Delamarre, Claudine Pique, Isabelle Le Blanc, Graziella Griffith, and Marie-Christine Dokhélar. "Early Assembly Step of a Retroviral Envelope Glycoprotein: Analysis Using a Dominant Negative Assay." Journal of Cell Biology 145, no. 1 (1999): 57–68. http://dx.doi.org/10.1083/jcb.145.1.57.

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As for most integral membrane proteins, the intracellular transport of retroviral envelope glycoproteins depends on proper folding and oligomeric assembly in the ER. In this study, we considered the hypothesis that a panel of 22 transport-defective mutants of the human T cell leukemia virus type 1 envelope glycoprotein might be defective in ER assembly. Upon cell cotransfection with wild-type envelope, however, the vast majority of these transport-defective mutants (21 of 22) exerted a specific trans-dominant negative effect. This effect was due to random dimerization of the mutated and wild-t

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Culp, D. J., L. R. Latchney, M. W. Frampton, M. R. Jahnke, P. E. Morrow, and M. J. Utell. "Composition of human airway mucins and effects after inhalation of acid aerosol." American Journal of Physiology-Lung Cellular and Molecular Physiology 269, no. 3 (1995): L358—L370. http://dx.doi.org/10.1152/ajplung.1995.269.3.l358.

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Characterization of normal airway mucus is required to elucidate mechanisms protecting the airways and to understand changes associated with disease and environmental insult. Toward this goal, we collected bronchial washes (10 ml saline) from healthy human subjects to 1) evaluate the yield of high-density material (delta > or = 1.35 g/ml), and 2) characterize glycoconjugates associated with collected secretions. Samples were lipid extracted followed by CsCl density gradient centrifugation. The yield of high-density material from individual subjects was variable but sufficient to demonstrate

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Wang, Qiong, and Michael J. Betenbaugh. "Metabolic engineering of CHO cells to prepare glycoproteins." Emerging Topics in Life Sciences 2, no. 3 (2018): 433–42. http://dx.doi.org/10.1042/etls20180056.

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As a complex and common post-translational modification, N-linked glycosylation affects a recombinant glycoprotein's biological activity and efficacy. For example, the α1,6-fucosylation significantly affects antibody-dependent cellular cytotoxicity and α2,6-sialylation is critical for antibody anti-inflammatory activity. Terminal sialylation is important for a glycoprotein's circulatory half-life. Chinese hamster ovary (CHO) cells are currently the predominant recombinant protein production platform, and, in this review, the characteristics of CHO glycosylation are summarized. Moreover, recent

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Wu, R., C. G. Plopper, and P. W. Cheng. "Mucin-like glycoprotein secreted by cultured hamster tracheal epithelial cells. Biochemical and immunological characterization." Biochemical Journal 277, no. 3 (1991): 713–18. http://dx.doi.org/10.1042/bj2770713.

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We isolated mucin-like glycoproteins from the conditioned medium of primary hamster tracheal epithelial (HTE) cell culture and characterized them biochemically and immunologically. These glycoproteins were purified on Sepharose CL-4B after Streptomyces hyaluronidase treatment and then by CsCl-density-gradient centrifugation in the presence of 4 M-guanidinium chloride. The purified glycoproteins were resistant to digestion by chondroitin AC lyase, heparinase, heparitinase and endo-N-acetylglucosaminidases A, D and H, but susceptible to endo-beta-galactosidase and keratanase. SDS/PAGE demonstrat

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Garry, Courtney E., та Robert F. Garry. "Proteomics Computational Analyses Suggest that the Antennavirus Glycoprotein Complex Includes a Class I Viral Fusion Protein (α-Penetrene) with an Internal Zinc-Binding Domain and a Stable Signal Peptide". Viruses 11, № 8 (2019): 750. http://dx.doi.org/10.3390/v11080750.

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A metatranscriptomic study of RNA viruses in cold-blooded vertebrates identified two related viruses from frogfish (Antennarius striatus) that represent a new genus Antennavirus in the family Arenaviridae (Order: Bunyavirales). Computational analyses were used to identify features common to class I viral fusion proteins (VFPs) in antennavirus glycoproteins, including an N-terminal fusion peptide, two extended alpha-helices, an intrahelical loop, and a carboxyl terminal transmembrane domain. Like mammarenavirus and hartmanivirus glycoproteins, the antennavirus glycoproteins have an intracellula

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Hortin, G., E. D. Green, J. U. Baenziger та A. W. Strauss. "Sulphation of proteins secreted by a human hepatoma-derived cell line. Sulphation of N-linked oligosaccharides on α2HS-glycoprotein". Biochemical Journal 235, № 2 (1986): 407–14. http://dx.doi.org/10.1042/bj2350407.

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Several human glycoproteins, including alpha 1-antitrypsin, alpha 1-acid glycoprotein, transferrin, caeruloplasmin and alpha 2HS-glycoprotein, synthesized by the hepatoma-derived cell line HepG2 were observed to contain covalently linked sulphate. These proteins were estimated to contain about 0.1 mol of sulphate/mol of protein. The most abundant of the sulphated glycoproteins, alpha 2HS-glycoprotein, was analysed in detail. All of the sulphate on this protein was attached to N-linked oligosaccharides which contained sialic acid and resisted release by endoglycosidase H. Several independent an

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Kassa, Aemro, Andrés Finzi, Marie Pancera, Joel R. Courter, Amos B. Smith, and Joseph Sodroski. "Identification of a Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Variant Resistant to Cold Inactivation." Journal of Virology 83, no. 9 (2009): 4476–88. http://dx.doi.org/10.1128/jvi.02110-08.

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ABSTRACT The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein trimer consists of gp120 and gp41 subunits and undergoes a series of conformational changes upon binding to the receptors, CD4 and CCR5/CXCR4, that promote virus entry. Surprisingly, we found that the envelope glycoproteins of some HIV-1 strains are functionally inactivated by prolonged incubation on ice. Serial exposure of HIV-1 to extremes of temperature, followed by expansion of replication-competent viruses, allowed selection of a temperature-resistant virus. The envelope glycoproteins of this virus resisted col

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Snyder, Aleksandra, Katarina Polcicova, and David C. Johnson. "Herpes Simplex Virus gE/gI and US9 Proteins Promote Transport of both Capsids and Virion Glycoproteins in Neuronal Axons." Journal of Virology 82, no. 21 (2008): 10613–24. http://dx.doi.org/10.1128/jvi.01241-08.

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ABSTRACT Following reactivation from latency, alphaherpesviruses replicate in sensory neurons and assemble capsids that are transported in the anterograde direction toward axon termini for spread to epithelial tissues. Two models currently describe this transport. The Separate model suggests that capsids are transported in axons independently from viral envelope glycoproteins. The Married model holds that fully assembled enveloped virions are transported in axons. The herpes simplex virus (HSV) membrane glycoprotein heterodimer gE/gI and the US9 protein are important for virus anterograde spre

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Lamers, Susanna L., Ruchi M. Newman, Oliver Laeyendecker, et al. "Global Diversity within and between Human Herpesvirus 1 and 2 Glycoproteins." Journal of Virology 89, no. 16 (2015): 8206–18. http://dx.doi.org/10.1128/jvi.01302-15.

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ABSTRACTHuman herpes simplex viruses 1 and 2 (HSV-1 and HSV-2) are large-genome DNA viruses that establish a persistent infection in sensory neurons and commonly manifest with recurring oral or genital erosions that transmit virus. HSV encodes 12 predicted glycoproteins that serve various functions, including cellular attachment, entry, and egress. Glycoprotein G is currently the target of an antibody test to differentiate HSV-1 from HSV-2; however, this test has shown reduced capacity to differentiate HSV strains in East Africa. Until the recent availability of 26 full-length HSV-1 and 36 ful

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Stein, W. D. "Kinetics of the multidrug transporter (P-glycoprotein) and its reversal." Physiological Reviews 77, no. 2 (1997): 545–90. http://dx.doi.org/10.1152/physrev.1997.77.2.545.

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Most cancer deaths result from the cancer's either being intrinsically resistant to chemotherapeutic drugs or becoming resistant after being initially sensitive. Often, in cells grown in cell culture, drug resistance correlates with the presence of one or more of the so-called P-glycoproteins or multidrug resistance proteins, products of the mdr family of genes. This review is largely concerned with the transport kinetics of the P-glycoproteins. We first present a brief overview of the P-glycoproteins, their properties, and their clinical significance. Later sections of the review expand on th

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Lin, Borong, Xue Qing, Jinling Liao, and Kan Zhuo. "Role of Protein Glycosylation in Host-Pathogen Interaction." Cells 9, no. 4 (2020): 1022. http://dx.doi.org/10.3390/cells9041022.

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Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promo

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Bowden, Thomas A., Max Crispin, Stephen C. Graham, et al. "Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein." Journal of Virology 83, no. 16 (2009): 8259–65. http://dx.doi.org/10.1128/jvi.00761-09.

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ABSTRACT New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel α/β fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown

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Jiang, Lingdong, Rui Lu, and Lei Ye. "Towards Detection of Glycoproteins Using Molecularly Imprinted Nanoparticles and Boronic Acid-Modified Fluorescent Probe." Polymers 11, no. 1 (2019): 173. http://dx.doi.org/10.3390/polym11010173.

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Glycoproteins represent a group of important biomarkers for cancer and other life-threatening diseases. Selective detection of specific glycoproteins is an important step for early diagnosis. Traditional glycoprotein assays are mostly based on lectins, antibodies, and enzymes, biochemical reagents that are costly and require special cold chain storage and distribution. To address the shortcomings of the existing glycoprotein assays, we propose a new approach using protein-imprinted nanoparticles to replace the traditional lectins and antibodies. Protein-imprinted binding sites were created on

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KONRAD, Zvia, and Jerry EICHLER. "Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation." Biochemical Journal 366, no. 3 (2002): 959–64. http://dx.doi.org/10.1042/bj20020757.

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Once the newly synthesized surface (S)-layer glycoprotein of the halophilic archaeaon Haloferax volcanii has traversed the plasma membrane, the protein undergoes a membrane-related, Mg2+-dependent maturation event, revealed as an increase in the apparent molecular mass and hydrophobicity of the protein. To test whether lipid modification of the S-layer glycoprotein could explain these observations, H. volcanii cells were incubated with a radiolabelled precursor of isoprene, [3H]mevalonic acid. In Archaea, isoprenoids serve as the major hydrophobic component of archaeal membrane lipids and have

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Batonick, Melissa, Antonius G. P. Oomens, and Gail W. Wertz. "Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells." Journal of Virology 82, no. 17 (2008): 8664–72. http://dx.doi.org/10.1128/jvi.00827-08.

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ABSTRACT Human respiratory syncytial virus (HRSV) is released from the apical membrane of polarized epithelial cells. However, little is known about the processes of assembly and release of HRSV and which viral gene products are involved in the directional maturation of the virus. Based on previous studies showing that the fusion (F) glycoprotein contained an intrinsic apical sorting signal and that N- and O-linked glycans can act as apical targeting signals, we investigated whether the glycoproteins of HRSV were involved in its directional targeting and release. We generated recombinant virus

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Santos, Joy Ramielle L., Weijie Sun, Tarana A. Mangukia, Eduardo Reyes-Serratos, and Marcelo Marcet-Palacios. "Challenging the Existing Model of the Hexameric HIV-1 Gag Lattice and MA Shell Superstructure: Implications for Viral Entry." Viruses 13, no. 8 (2021): 1515. http://dx.doi.org/10.3390/v13081515.

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Despite type 1 human immunodeficiency virus (HIV-1) being discovered in the early 1980s, significant knowledge gaps remain in our understanding of the superstructure of the HIV-1 matrix (MA) shell. Current viral assembly models assume that the MA shell originates via recruitment of group-specific antigen (Gag) polyproteins into a hexagonal lattice but fails to resolve and explain lattice overlapping that occurs when the membrane is folded into a spherical/ellipsoidal shape. It further fails to address how the shell recruits, interacts with and encompasses the viral spike envelope (Env) glycopr

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Wahl-Jensen, Victoria, Sabine K. Kurz, Paul R. Hazelton, et al. "Role of Ebola Virus Secreted Glycoproteins and Virus-Like Particles in Activation of Human Macrophages." Journal of Virology 79, no. 4 (2005): 2413–19. http://dx.doi.org/10.1128/jvi.79.4.2413-2419.2005.

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ABSTRACT Ebola virus, a member of the family Filoviridae, causes one of the most severe forms of viral hemorrhagic fever. In the terminal stages of disease, symptoms progress to hypotension, coagulation disorders, and hemorrhages, and there is prominent involvement of the mononuclear phagocytic and reticuloendothelial systems. Cells of the mononuclear phagocytic system are primary target cells and producers of inflammatory mediators. Ebola virus efficiently produces four soluble glycoproteins during infection: sGP, delta peptide (Δ-peptide), GP1, and GP1,2Δ. While the presence of these glycopr

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