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Journal articles on the topic 'Envelope protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Pan, Yong, Jiming Yan, Yinong Zhang, Jiasheng Lin, Zhiquan Liang, and Jingchen Sun. "Centrifugation-Based Purification Protocol Optimization Enhances Structural Preservation of Nucleopolyhedrovirus Budded Virion Envelopes." Insects 16, no. 4 (2025): 424. https://doi.org/10.3390/insects16040424.

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The structural integrity of viral envelopes is a critical determinant of infectivity for enveloped viruses, directly influencing vector stability, functional accuracy of surface-displayed epitopes, and preservation of native conformational states required for membrane protein studies. However, conventional purification methods often disrupt envelope integrity and cause envelope proteins to lose their activity. Here, we systematically compared discontinuous, continuous, and optimized continuous sucrose density gradient centrifugation protocols for purifying Autographa californica multiple nucle

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2

Kalmokoff, M. L., J. W. Austin, M. F. Whitford, and R. M. Teather. "Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268." Canadian Journal of Microbiology 46, no. 4 (2000): 295–303. http://dx.doi.org/10.1139/w99-149.

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Cell envelopes from the Gram-negative staining but phylogenetically Gram-positive rumen anaerobe Selenomonas ruminantium OB268 contained a major 42 kDa heat modifiable protein. A similarly sized protein was present in the envelopes of Selenomonas ruminantium D1 and Selenomonas infelix. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of Triton X-100 extracted cell envelopes from S. ruminantium OB268 showed that they consisted primarily of the 42 kDa protein. Polyclonal antisera produced against these envelopes cross-reacted only with the 42 kDa major envelope proteins in both S. rumin

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3

Huang, Po-Yu, Jiann-Horng Leu, and Li-Li Chen. "A newly identified protein complex that mediates white spot syndrome virus infection via chitin-binding protein." Journal of General Virology 95, no. 8 (2014): 1799–808. http://dx.doi.org/10.1099/vir.0.064782-0.

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White spot syndrome virus (WSSV) is a large enveloped virus which has caused severe mortality and huge economic losses in the shrimp farming industry. The enveloped virus must be combined with the receptors of the host cell membrane by the virus envelope proteins. In the case of WSSV, binding of envelope proteins with receptors of the host cell membrane was discovered in a number of previous studies, such as VP53A and 10 other proteins with chitin-binding protein (CBP), VP28 with Penaeus monodon Rab7, VP187 with β-integrin, and so on. WSSV envelope proteins were also considered capable of form

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4

Lin, Lo-Wei, Michael S. Denison, and Robert H. Rice. "Woodsmoke Extracts Cross-Link Proteins and Induce Cornified Envelope Formation without Stimulating Keratinocyte Terminal Differentiation." Toxicological Sciences 183, no. 1 (2021): 128–38. http://dx.doi.org/10.1093/toxsci/kfab071.

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Abstract Air pollution poses a serious risk to human health. To help understand the contribution of smoke from wood burning to the harmfulness of air pollution toward the skin, we studied the effects of liquid smoke, aqueous extracts of wood smoke condensate, a commercially available food flavor additive, in cultured keratinocytes. We report that liquid smoke can react with and cross-link keratinocyte cellular proteins, leading to abnormal cross-linked envelope formation. Instead of inducing genes ordinarily involved in terminal differentiation, liquid smoke induced expression of genes associa

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van Hulten, Mariëlle C. W., Martin Reijns, Angela M. G. Vermeesch, Fokko Zandbergen, and Just M. Vlak. "Identification of VP19 and VP15 of white spot syndrome virus (WSSV) and glycosylation status of the WSSV major structural proteins." Journal of General Virology 83, no. 1 (2002): 257–65. http://dx.doi.org/10.1099/0022-1317-83-1-257.

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White spot syndrome virus (WSSV) infects penaeid shrimp and other crustaceans. The WSSV virion consists of an enveloped rod-shaped nucleocapsid enclosing a large circular double-stranded DNA genome of 293 kbp. The virion envelope contains two major proteins of 28 (VP28) and 19 kDa (VP19) and the nucleocapsid consists of three major proteins of 26 (VP26), 24 (VP24) and 15 kDa (VP15). Study on the morphogenesis of the WSSV particle requires the genomic identification and chemical characterization of these WSSV virion proteins. An internal amino acid sequence of envelope protein VP19 was obtained

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6

Hyllner, S. J., and C. Haux. "Immunochemical detection of the major vitelline envelope proteins in the plasma and oocytes of the maturing female rainbow trout, Oncorhynchus mykiss." Journal of Endocrinology 135, no. 2 (1992): 303—NP. http://dx.doi.org/10.1677/joe.0.1350303.

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ABSTRACT The major vitelline envelope proteins were detected in the plasma of female rainbow trout maturing under natural conditions by using the Western blot technique. Females were sampled every month from July until ovulation in January. The amount of vitelline envelope proteins in plasma increased markedly as the gonads increased in size from 0·4 to about 15% of the total body weight. The plasma level of oestradiol-17β largely followed the alterations in the amount of vitelline envelope proteins, indicating the endocrine control of vitelline envelope protein synthesis. In addition, plasma

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7

Granzow, Harald, Barbara G. Klupp, and Thomas C. Mettenleiter. "The Pseudorabies Virus US3 Protein Is a Component of Primary and of Mature Virions." Journal of Virology 78, no. 3 (2004): 1314–23. http://dx.doi.org/10.1128/jvi.78.3.1314-1323.2004.

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ABSTRACT Herpesviruses acquire a primary envelope by budding of capsids at the inner leaflet of the nuclear membrane. They then traverse into the cytoplasm after fusion of the primary envelope with the outer leaflet of the nuclear membrane. In the alphaherpesvirus pseudorabies virus (PrV), the latter process is impaired when the US3 protein is absent. Acquisition of final tegument and envelope occurs in the cytoplasm. Besides the capsid components, only the UL31 and UL34 gene products of PrV have unequivocally been shown to be part of primary enveloped virions, whereas they lack several tegume

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8

Hu, Dingwen, Haimei Zou, Weijie Chen, et al. "ZDHHC11 Suppresses Zika Virus Infections by Palmitoylating the Envelope Protein." Viruses 15, no. 1 (2023): 144. http://dx.doi.org/10.3390/v15010144.

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Zika virus (ZIKV) is an RNA-enveloped virus that belongs to the Flavivirus genus, and ZIKV infections potentially induce severe neurodegenerative diseases and impair male fertility. Palmitoylation is an important post-translational modification of proteins that is mediated by a series of DHHC-palmitoyl transferases, which are implicated in various biological processes and viral infections. However, it remains to be investigated whether palmitoylation regulates ZIKV infections. In this study, we initially observed that the inhibition of palmitoylation by 2-bromopalmitate (2-BP) enhanced ZIKV in

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9

Courvalin, J. C., K. Lassoued, H. J. Worman, and G. Blobel. "Identification and characterization of autoantibodies against the nuclear envelope lamin B receptor from patients with primary biliary cirrhosis." Journal of Experimental Medicine 172, no. 3 (1990): 961–67. http://dx.doi.org/10.1084/jem.172.3.961.

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We have identified autoantibodies from two patients with primary biliary cirrhosis (PBC) that recognize the nuclear envelope of mammalian cells on indirect immunofluorescence microscopy. These antibodies bind to a 58-kD integral membrane protein (p58) of the turkey erythrocyte nuclear envelope, which has been previously identified as a membrane receptor for lamin B (Worman, H. J., J. Yuan, G. Blobel, and S. D. Georgatos. 1988. Proc. Natl. Acad. Sci. USA. 85:8531). The antibodies also bind to a 61-kD integral membrane protein (p61) of the rat liver nuclear envelope. Affinity-purified antibodies

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10

Frank, John A., Manvendra Singh, Harrison B. Cullen, et al. "Evolution and antiviral activity of a human protein of retroviral origin." Science 378, no. 6618 (2022): 422–28. http://dx.doi.org/10.1126/science.abq7871.

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Endogenous retroviruses are abundant components of mammalian genomes descended from ancient germline infections. In several mammals, the envelope proteins encoded by these elements protect against exogenous viruses, but this activity has not been documented with endogenously expressed envelopes in humans. We report that the human genome harbors a large pool of envelope-derived sequences with the potential to restrict retroviral infection. To test this, we characterized an envelope-derived protein, Suppressyn. We found that Suppressyn is expressed in human preimplantation embryos and developing

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11

Wieringa, Roeland, Antoine A. F. de Vries, Sabine M. Post, and Peter J. M. Rottier. "Intra- and Intermolecular Disulfide Bonds of theGP2b Glycoprotein of Equine Arteritis Virus: Relevance forVirus Assembly andInfectivity." Journal of Virology 77, no. 24 (2003): 12996–3004. http://dx.doi.org/10.1128/jvi.77.24.12996-13004.2003.

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ABSTRACT Equine arteritis virus (EAV) is an enveloped, positive-strand RNA virus belonging to the family Arteriviridae of the order Nidovirales. EAV virions contain six different envelope proteins. The glycoprotein GP5 (previously named GL) and the unglycosylated membrane protein M are the major envelope proteins, while the glycoproteins GP2b (previously named GS), GP3, and GP4 are minor structural proteins. The unglycosylated small hydrophobic envelope protein E is present in virus particles in intermediate molar amounts compared to the other transmembrane proteins. The GP5 and M proteins are

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12

Fleming, Elisa H., Andrey A. Kolokoltsov, Robert A. Davey, Joan E. Nichols, and Norbert J. Roberts. "Respiratory Syncytial Virus F Envelope Protein Associates with Lipid Rafts without a Requirement for Other Virus Proteins." Journal of Virology 80, no. 24 (2006): 12160–70. http://dx.doi.org/10.1128/jvi.00643-06.

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ABSTRACT Like many enveloped viruses, human respiratory syncytial virus (RSV) assembles at and buds from lipid rafts. Translocation of the envelope proteins to these membrane subdomains is essential for production of infectious virus, but the targeting mechanism is poorly understood and it is not known if other virus proteins are required. Here we demonstrate that F protein of RSV intrinsically targets to lipid rafts without a requirement for any other virus protein, including the SH and G envelope proteins. Recombinant virus deficient in SH and G but retaining F protein expression was used to

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13

Blaise, Sandra, Alessia Ruggieri, Marie Dewannieux, François-Loic Cosset, and Thierry Heidmann. "Identification of an Envelope Protein from the FRD Family of Human Endogenous Retroviruses (HERV-FRD) Conferring Infectivity and Functional Conservation among Simians." Journal of Virology 78, no. 2 (2004): 1050–54. http://dx.doi.org/10.1128/jvi.78.2.1050-1054.2004.

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ABSTRACT A member of the HERV-W family of human endogenous retroviruses (HERV) had previously been demonstrated to encode a functional envelope which can form pseudotypes with human immunodeficiency virus type 1 virions and confer infectivity on the resulting retrovirus particles. Here we show that a second envelope protein sorted out by a systematic search for fusogenic proteins that we made among all the HERV coding envelope genes and belonging to the HERV-FRD family can also make pseudotypes and confer infectivity. We further show that the orthologous envelope genes that were isolated from

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14

Wilson, K. L., and J. Newport. "A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro." Journal of Cell Biology 107, no. 1 (1988): 57–68. http://dx.doi.org/10.1083/jcb.107.1.57.

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The reformation of functioning organelles at the end of mitosis presents a problem in vesicle targeting. Using extracts made from Xenopus laevis frog eggs, we have studied in vitro the vesicles that reform the nuclear envelope. In the in vitro assay, nuclear envelope growth is linear with time. Furthermore, the final surface area of the nuclear envelopes formed is directly dependent upon the amount of membrane vesicles added to the assay. Egg membrane vesicles could be fractionated into two populations, only one of which was competent for nuclear envelope assembly. We found that vesicles activ

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15

Husain, Matloob, and Bernard Moss. "Role of Receptor-Mediated Endocytosis in the Formation of Vaccinia Virus Extracellular Enveloped Particles." Journal of Virology 79, no. 7 (2005): 4080–89. http://dx.doi.org/10.1128/jvi.79.7.4080-4089.2005.

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ABSTRACT Infectious intracellular mature vaccinia virus particles are wrapped by cisternae, which may arise from trans-Golgi or early endosomal membranes, and are transported along microtubules to the plasma membrane where exocytosis occurs. We used EH21, a dominant-negative form of Eps15 that is an essential component of clathrin-coated pits, to investigate the extent and importance of endocytosis of viral envelope proteins from the cell surface. Several recombinant vaccinia viruses that inducibly or constitutively express an enhanced green fluorescent protein (GFP)-EH21 fusion protein were c

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16

Xie, Xixian, and Feng Yang. "White spot syndrome virus VP24 interacts with VP28 and is involved in virus infection." Journal of General Virology 87, no. 7 (2006): 1903–8. http://dx.doi.org/10.1099/vir.0.81570-0.

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White spot syndrome virus (WSSV) is one of the most virulent pathogens causing high mortality in shrimp. Herein, the characterization of VP24, a major structural protein of WSSV, is described. When purified virions were subjected to Nonidet P-40 treatment to separate the envelopes from the nucleocapsids, VP24 was found to be present exclusively in the envelope fraction. Triton X-114 extraction also indicated that VP24 behaves as an envelope protein. Immunoelectron microscopy further confirmed that VP24 is located in the virion envelope. Far-Western experiments showed that VP24 interacts with V

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17

Lord, J. M., J. A. Thick, C. M. Bunce, et al. "Characterization of a novel nuclear envelope protein restricted to certain cell types." Journal of Cell Science 90, no. 2 (1988): 237–45. http://dx.doi.org/10.1242/jcs.90.2.237.

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The monoclonal antibody AGF2.3 identifies a nuclear envelope protein that is restricted to certain cell types. In particular, this antigen shows a reduced level of expression during haemopoietic cell maturation. In this study, we have examined the relationship of this protein to known nuclear envelope proteins that have a similar molecular mass. Antigen extraction and immunoelectron microscope studies revealed that the AGF2.3 protein is an integral membrane protein present at both the inner and outer aspects of the nuclear envelope. The protein is not associated with nuclear pores and therefor

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Klingen, Yvonne, Karl-Klaus Conzelmann, and Stefan Finke. "Double-Labeled Rabies Virus: Live Tracking of Enveloped Virus Transport." Journal of Virology 82, no. 1 (2007): 237–45. http://dx.doi.org/10.1128/jvi.01342-07.

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ABSTRACT Here we describe a strategy to fluorescently label the envelope of rabies virus (RV), of the Rhabdoviridae family, in order to track the transport of single enveloped viruses in living cells. Red fluorescent proteins (tm-RFP) were engineered to comprise the N-terminal signal sequence and C-terminal transmembrane spanning and cytoplasmic domain sequences of the RV glycoprotein (G). Two variants of tm-RFP were transported to and anchored in the cell surface membrane, independent of glycosylation. As shown by confocal microscopy, tm-RFP colocalized at the cell surface with the RV matrix

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Schleiff, Enrico, Roselynn Tien, Michael Salomon, and Jürgen Soll. "Lipid Composition of Outer Leaflet of Chloroplast Outer Envelope Determines Topology of OEP7." Molecular Biology of the Cell 12, no. 12 (2001): 4090–102. http://dx.doi.org/10.1091/mbc.12.12.4090.

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OEP7, a 6.7-kDa outer envelope protein of spinach chloroplasts inserts into the outer envelope of the organelle independent of a classical cleavable targeting signal. The insertion of OEP7 was studied to describe the determinants for association with, integration into, and orientation of the protein in the outer envelope of chloroplasts. The insertion of OEP7 into the membrane is independent of outer membrane channel proteins and can be reconstituted with the use of protein-free liposomes. In situ, the binding of OEP7 to the membrane surface is not driven by electrostatic interaction because r

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20

Narayanan, Krishna, Chun-Jen Chen, Junko Maeda, and Shinji Makino. "Nucleocapsid-Independent Specific Viral RNA Packaging via Viral Envelope Protein and Viral RNA Signal." Journal of Virology 77, no. 5 (2003): 2922–27. http://dx.doi.org/10.1128/jvi.77.5.2922-2927.2003.

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ABSTRACT For any of the enveloped RNA viruses studied to date, recognition of a specific RNA packaging signal by the virus's nucleocapsid (N) protein is the first step described in the process of viral RNA packaging. In the murine coronavirus a selective interaction between the viral transmembrane envelope protein M and the viral ribonucleoprotein complex, composed of N protein and viral RNA containing a short cis-acting RNA element, the packaging signal, determines the selective RNA packaging into virus particles. In this report we show that expressed coronavirus envelope protein M specifical

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Chi, N. C., E. J. Adam, and S. A. Adam. "Sequence and characterization of cytoplasmic nuclear protein import factor p97." Journal of Cell Biology 130, no. 2 (1995): 265–74. http://dx.doi.org/10.1083/jcb.130.2.265.

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Nuclear location sequence-mediated binding of karyophilic proteins to the nuclear pore complexes is one of the earliest steps in nuclear protein import. We previously identified two cytosolic proteins that reconstitute this step in a permeabilized cell assay: the 54/56-kD NLS receptor and p97. A monoclonal antibody to p97 localizes the protein to the cytoplasm and the nuclear envelope. p97 is extracted from nuclear envelopes under the same conditions as the O-glycosylated nucleoporins indicating a tight association with the pore complex. The antibody inhibits import in a permeabilized cell ass

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Schröder, H. C., M. Rottmann, R. Wenger, M. Bachmann, A. Dorn, and W. E. G. Müller. "Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport." Biochemical Journal 252, no. 3 (1988): 777–90. http://dx.doi.org/10.1042/bj2520777.

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The rate of energy-dependent nucleoside triphosphatase (NTPase)-mediated nucleocytoplasmic translocation of poly(A)-containing mRNA [poly(A)+mRNA] across the nuclear envelope is thought to be regulated by poly(A)-sensitive phosphorylation and dephosphorylation of nuclear-envelope protein. Studying the phosphorylation-related inhibition of the NTPase, we found that phosphorylation of one polypeptide of rat liver envelopes by endogenous NI- and NII-like protein kinase was particularly sensitive to poly(A). This polypeptide (106 kDa) was also phosphorylated by nuclear-envelope-bound Ca2+-activate

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Lorenzo, María M., Juana M. Sánchez-Puig, and Rafael Blasco. "Mutagenesis of the palmitoylation site in vaccinia virus envelope glycoprotein B5." Journal of General Virology 93, no. 4 (2012): 733–43. http://dx.doi.org/10.1099/vir.0.039016-0.

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The outer envelope of vaccinia virus extracellular virions is derived from intracellular membranes that, at late times in infection, are enriched in several virus-encoded proteins. Although palmitoylation is common in vaccinia virus envelope proteins, little is known about the role of palmitoylation in the biogenesis of the enveloped virus. We have studied the palmitoylation of B5, a 42 kDa type I transmembrane glycoprotein comprising a large ectodomain and a short (17 aa) cytoplasmic tail. Mutation of two cysteine residues located in the cytoplasmic tail in close proximity to the transmembran

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Fu, Ruijiang, Wu-Pei Su, and Hongxing He. "Refining Protein Envelopes with a Transition Region for Enhanced Direct Phasing in Protein Crystallography." Crystals 14, no. 1 (2024): 85. http://dx.doi.org/10.3390/cryst14010085.

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In protein crystallography, the determination of an accurate protein envelope is of paramount importance for ab initio phasing of diffraction data. In our previous work, we introduced an approach to ascertain the protein envelope by seeking an optimal cutoff value on a weighted-average density map. In this paper, we present a significant advancement in our approach by focusing on identifying a transition region that demarcates the boundary between the protein and solvent regions, rather than relying solely on a single cutoff value. Within this transition region, we conducted a meticulous searc

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Lorenzo, María M., Inmaculada Galindo, Gareth Griffiths, and Rafael Blasco. "Intracellular Localization of Vaccinia Virus Extracellular Enveloped Virus Envelope Proteins Individually Expressed Using a Semliki Forest Virus Replicon." Journal of Virology 74, no. 22 (2000): 10535–50. http://dx.doi.org/10.1128/jvi.74.22.10535-10550.2000.

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ABSTRACT The extracellular enveloped virus (EEV) form of vaccinia virus is bound by an envelope which is acquired by wrapping of intracellular virus particles with cytoplasmic vesicles containing trans-Golgi network markers. Six virus-encoded proteins have been reported as components of the EEV envelope. Of these, four proteins (A33R, A34R, A56R, and B5R) are glycoproteins, one (A36R) is a nonglycosylated transmembrane protein, and one (F13L) is a palmitylated peripheral membrane protein. During infection, these proteins localize to the Golgi complex, where they are incorporated into infectiou

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Paul, Prisho Mariam, Krupakar Parthasarathy, Sudhanarayani S Rao, and Vignesh Sounderrajan. "In silico Docking Analysis of the FDA-Approved Drugs on Envelope Protein of SARS CoV-2 Omicron Variant." Biomedical and Pharmacology Journal 16, no. 4 (2023): 1989–96. http://dx.doi.org/10.13005//bpj/2775.

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The current pandemic situation is created by the highly evolving SARS coronavirus 2 which is having several mutations in its structural proteins. The structural proteins of SARS CoV-2 include spike (S), Envelope (E), Membrane (M), and Nucleocapsid (N) which are primarily responsible for the infection, transmission, and pathogenesis of the virus. Envelope protein is the smallest of the four proteins containing 75 amino acids with a molecular weight of about 8 kDa. The major functions of the hydrophobic envelope protein include envelope formation, budding, replication, and release of the virion.

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Noegel, Angelika A., and Sascha Neumann. "The role of nesprins as multifunctional organizers in the nucleus and the cytoskeleton." Biochemical Society Transactions 39, no. 6 (2011): 1725–28. http://dx.doi.org/10.1042/bst20110668.

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Nesprins (nuclear envelope spectrin repeat proteins), also known as SYNE (synaptic nuclear envelope protein), MYNE (myocyte nuclear envelope protein), ENAPTIN and NUANCE, are proteins that are primarily components of the nuclear envelope. The nuclear envelope is a continuous membrane system composed of two lipid bilayers: an inner and an outer nuclear membrane. Nesprins are components of both nuclear membranes and reach into the nucleoplasm and the cytoplasm, where they undergo different interactions and have the potential to influence transcriptional processes and cytoskeletal activities.

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Ting, Yuan-Tsang, Carolyn A. Wilson, Karen B. Farrell, G. Jilani Chaudry, and Maribeth V. Eiden. "Simian Sarcoma-Associated Virus Fails To Infect Chinese Hamster Cells despite the Presence of Functional Gibbon Ape Leukemia Virus Receptors." Journal of Virology 72, no. 12 (1998): 9453–58. http://dx.doi.org/10.1128/jvi.72.12.9453-9458.1998.

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ABSTRACT We have sequenced the envelope genes from each of the five members of the gibbon ape leukemia virus (GALV) family of type C retroviruses. Four of the GALVs, including GALV strain SEATO (GALV-S), were originally isolated from gibbon apes, whereas the fifth member of this family, simian sarcoma-associated virus (SSAV), was isolated from a woolly monkey and shares 78% amino acid identity with GALV-S. To determine whether these viruses have identical host ranges, we evaluated the susceptibility of several cell lines to either GALV-S or SSAV infection. GALV-S and SSAV have the same host ra

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Zavorotinskaya, Tatiana, and Lorraine M. Albritton. "Failure To Cleave Murine Leukemia Virus Envelope Protein Does Not Preclude Its Incorporation in Virions and Productive Virus-Receptor Interaction." Journal of Virology 73, no. 7 (1999): 5621–29. http://dx.doi.org/10.1128/jvi.73.7.5621-5629.1999.

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ABSTRACT It is thought that complete cleavage of retroviral envelope protein into mature surface protein (SU) and transmembrane protein (TM) is critical for its assembly into virions and the formation of infectious virus particles. Here we report the identification of highly infectious, cleavage-deficient envelope mutant proteins. Substitution of aspartate for lysine 104, arginines 124 and 126, or arginines 223 and 225 strongly suppressed cleavage of the envelope precursor and yet allowed efficient incorporation of precursor molecules as the predominant species in virions that were almost as i

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Meier, Iris, Xiao Zhou, Jelena Brkljacić, Annkatrin Rose, Qiao Zhao, and Xianfeng Morgan Xu. "Targeting proteins to the plant nuclear envelope." Biochemical Society Transactions 38, no. 3 (2010): 733–40. http://dx.doi.org/10.1042/bst0380733.

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The nuclear envelope and the nuclear pore are important structures that both separate and selectively connect the nucleoplasm and the cytoplasm. The requirements for specific targeting of proteins to the plant nuclear envelope and nuclear pore are poorly understood. How are transmembrane-domain proteins sorted to the nuclear envelope and nuclear pore membranes? What protein–protein interactions are involved in associating other proteins to the nuclear pore? Are there plant-specific aspects to these processes? We are using the case of the nuclear pore-associated Ran-cycle component RanGAP (Ran

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Perdiguero, Beatriz, María M. Lorenzo, and Rafael Blasco. "Vaccinia Virus A34 Glycoprotein Determines the Protein Composition of the Extracellular Virus Envelope." Journal of Virology 82, no. 5 (2007): 2150–60. http://dx.doi.org/10.1128/jvi.01969-07.

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ABSTRACT The outer envelope of the extracellular form of vaccinia virus contains five virus-encoded proteins, F13, A33, A34, A56, and B5, that, with the exception of A56, are implicated in virus egress or infectivity. A34, a type II transmembrane glycoprotein, is involved in the induction of actin tails, the release of enveloped virus from the surfaces of infected cells, and the disruption of the virus envelope after ligand binding prior to virus entry. To investigate interactions between A34 and other envelope proteins, a recombinant vaccinia virus (vA34RHA) expressing an epitope-tagged versi

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Klupp, Barbara G., Harald Granzow, and Thomas C. Mettenleiter. "Primary Envelopment of Pseudorabies Virus at the Nuclear Membrane Requires the UL34 Gene Product." Journal of Virology 74, no. 21 (2000): 10063–73. http://dx.doi.org/10.1128/jvi.74.21.10063-10073.2000.

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ABSTRACT Primary envelopment of several herpesviruses has been shown to occur by budding of intranuclear capsids through the inner nuclear membrane. By subsequent fusion of the primary envelope with the outer nuclear membrane, capsids are released into the cytoplasm and gain their final envelope by budding into vesicles in thetrans-Golgi area. We show here that the product of the UL34 gene of pseudorabies virus, an alphaherpesvirus of swine, is localized in transfected and infected cells in the nuclear membrane. It is also detected in the envelope of virions in the perinuclear space but is und

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Spilman, Michael S., Craig Welbon, Eric Nelson, and Terje Dokland. "Cryo-electron tomography of porcine reproductive and respiratory syndrome virus: organization of the nucleocapsid." Journal of General Virology 90, no. 3 (2009): 527–35. http://dx.doi.org/10.1099/vir.0.007674-0.

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Porcine reproductive and respiratory virus (PRRSV) is an enveloped positive-sense RNA virus of the family Arteriviridae that causes severe and persistent disease in pigs worldwide. The PRRSV virion consists of a lipid envelope that contains several envelope proteins surrounding a nucleocapsid core that encapsidates the RNA genome. To provide a better understanding of the structure and assembly of PRRSV, we have carried out cryo-electron microscopy and tomographic reconstruction of virions grown in MARC-145 cells. The virions are pleomorphic, round to egg-shaped particles with an average diamet

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Kariithi, Henry M., Jan W. M. van Lent, Sjef Boeren, et al. "Correlation between structure, protein composition, morphogenesis and cytopathology of Glossina pallidipes salivary gland hypertrophy virus." Journal of General Virology 94, no. 1 (2013): 193–208. http://dx.doi.org/10.1099/vir.0.047423-0.

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The Glossina pallidipes salivary gland hypertrophy virus (GpSGHV) is a dsDNA virus with rod-shaped, enveloped virions. Its 190 kb genome contains 160 putative protein-coding ORFs. Here, the structural components, protein composition and associated aspects of GpSGHV morphogenesis and cytopathology were investigated. Four morphologically distinct structures: the nucleocapsid, tegument, envelope and helical surface projections, were observed in purified GpSGHV virions by electron microscopy. Nucleocapsids were present in virogenic stroma within the nuclei of infected salivary gland cells, whereas

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Marraffini, Luciano A., Andrea C. DeDent, and Olaf Schneewind. "Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria." Microbiology and Molecular Biology Reviews 70, no. 1 (2006): 192–221. http://dx.doi.org/10.1128/mmbr.70.1.192-221.2006.

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SUMMARY The cell wall envelopes of gram-positive bacteria represent a surface organelle that not only functions as a cytoskeletal element but also promotes interactions between bacteria and their environment. Cell wall peptidoglycan is covalently and noncovalently decorated with teichoic acids, polysaccharides, and proteins. The sum of these molecular decorations provides bacterial envelopes with species- and strain-specific properties that are ultimately responsible for bacterial virulence, interactions with host immune systems, and the development of disease symptoms or successful outcomes o

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Goldberg, Michal, Huihua Lu, Nico Stuurman, et al. "Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA." Molecular and Cellular Biology 18, no. 7 (1998): 4315–23. http://dx.doi.org/10.1128/mcb.18.7.4315.

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ABSTRACT The nuclear envelope plays many roles, including organizing nuclear structure and regulating nuclear events. Molecular associations of nuclear envelope proteins may contribute to the implementation of these functions. Lamin, otefin, and YA are the three Drosophilanuclear envelope proteins known in early embryos. We used the yeast two-hybrid system to explore the interactions between pairs of these proteins. The ubiquitous major lamina protein, lamin Dm, interacts with both otefin, a peripheral protein of the inner nuclear membrane, and YA, an essential, developmentally regulated prote

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Hennen, Jared, Cosmo A. Saunders, Joachim D. Mueller, and G. W. Gant Luxton. "Fluorescence fluctuation spectroscopy reveals differential SUN protein oligomerization in living cells." Molecular Biology of the Cell 29, no. 9 (2018): 1003–11. http://dx.doi.org/10.1091/mbc.e17-04-0233.

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Linker-of-nucleoskeleton-and-cytoskeleton (LINC) complexes are conserved molecular bridges within the nuclear envelope that mediate mechanical force transmission into the nucleoplasm. The core of a LINC complex is formed by a transluminal interaction between the outer and inner nuclear membrane KASH and SUN proteins, respectively. Mammals encode six KASH proteins and five SUN proteins. Recently, KASH proteins were shown to bind to the domain interfaces of trimeric SUN2 proteins in vitro. However, neither the existence of SUN2 trimers in living cells nor the extent to which other SUN proteins c

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Ezzell, Carol. "AIDS envelope protein patent." Nature 331, no. 6158 (1988): 649. http://dx.doi.org/10.1038/331649c0.

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Perdiguero, Beatriz, and Rafael Blasco. "Interaction between Vaccinia Virus Extracellular Virus Envelope A33 and B5 Glycoproteins." Journal of Virology 80, no. 17 (2006): 8763–77. http://dx.doi.org/10.1128/jvi.00598-06.

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ABSTRACT The extracellular form of vaccinia virus acquires its outer envelope by wrapping with cytoplasmic membranes that contain at least seven virus-encoded proteins, of which four are glycoproteins. We searched for interactions between the vaccinia virus A33 glycoprotein and proteins A34, A36, B5, F12, and F13. First, when myc epitope-tagged A33 was expressed in combination with other envelope proteins, A33 colocalized with B5 and A36, suggesting that direct A33-B5 and A33-A36 interactions occur in the absence of infection. A recombinant vaccinia virus (vA33Rmyc) was constructed by introduc

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Ha, Mihyang, Ji-Young Kim, Myoung-Eun Han, et al. "TMEM18: A Novel Prognostic Marker in Acute Myeloid Leukemia." Acta Haematologica 140, no. 2 (2018): 71–76. http://dx.doi.org/10.1159/000492742.

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Background: Certain nuclear envelope proteins are associated with important cancer cell characteristics, including migration and proliferation. Abnormal expression of and genetic changes in nuclear envelope proteins have been reported in acute myeloid leukemia (AML) patients. Transmembrane protein 18 (TMEM18), a nuclear envelope protein, is involved in neural stem cell migration and tumorigenicity. Methods: To examine the prognostic significance of TMEM18 in AML patients, we analyzed an AML cohort from The Cancer Genome Atlas (TCGA, n = 142). Results: Kaplan-Meier survival analysis revealed th

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Polanco, Carlos, Vladimir N. Uversky, Alberto Huberman, et al. "Dengue Fever Virus Envelope Glycoproteins Variability Characterized Bioinformatically." Current Analytical Chemistry 19, no. 9 (2023): 642–68. http://dx.doi.org/10.2174/0115734110260787231102101646.

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Background: The infection caused by the dengue fever virus is a severe threat to public health on a global scale; nevertheless, there is currently no effective medical treatment or vaccine available to prevent or treat the condition. Objective: To better understand the physicochemical regularities of these proteins, it is necessary to carry out a computational multiparametric study of the amino acid sequences of envelope proteins expressed by the dengue fever virus and obtain a bioinformatics method that can use the subsequences of the training protein group to figure out the preponderant func

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Chen, K., X. Chen, and D. J. Schnell. "Mechanism of protein import across the chloroplast envelope." Biochemical Society Transactions 28, no. 4 (2000): 485–91. http://dx.doi.org/10.1042/bst0280485.

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The development and maintenance of chloroplasts relies on the contribution of protein subunits from both plastid and nuclear genomes. Most chloroplast proteins are encoded by nuclear genes and are post-translationally imported into the organelle across the double membrane of the chloroplast envelope. Protein import into the chloroplast consists of two essential elements: the specific recognition of the targeting signals (transit sequences) of cytoplasmic preproteins by receptors at the outer envelope membrane and the subsequent translocation of preproteins simultaneously across the double memb

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Furukawa, Hiroto, Hiroshi Inaba, Yoshihiro Sasaki, Kazunari Akiyoshi, and Kazunori Matsuura. "Embedding a membrane protein into an enveloped artificial viral replica." RSC Chemical Biology 3, no. 2 (2022): 231–41. http://dx.doi.org/10.1039/d1cb00166c.

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We demonstrate the embedding membrane protein, Cx43, on the enveloped artificial viral capsid using a cell-free expression system. The embedding of Cx43 on the envelope was evaluated by detection with anti-Cx43 antibody using FCS and TEM.

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Gudima, Severin, Yiping He, Ning Chai, et al. "Primary Human Hepatocytes Are Susceptible to Infection by Hepatitis Delta Virus Assembled with Envelope Proteins of Woodchuck Hepatitis Virus." Journal of Virology 82, no. 15 (2008): 7276–83. http://dx.doi.org/10.1128/jvi.00576-08.

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ABSTRACT Hepatitis B virus (HBV) and hepatitis delta virus (HDV) share the HBV envelope proteins. When woodchucks chronically infected with woodchuck hepatitis virus (WHV) are superinfected with HDV, they produce HDV with a WHV envelope, wHDV. Several lines of evidence are provided that wHDV infects not only cultured primary woodchuck hepatocytes (PWH) but also primary human hepatocytes (PHH). Surprisingly, HBV-enveloped HDV (hHDV) and wHDV infected PHH with comparable efficiencies; however, hHDV did not infect PWH. The basis for these host range specificities was investigated using as inhibit

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Ruchi, Yadav. "Elucidating Structural, Functional and Phylogenetic Relationship of Large Envelope Protein of Hepatitis B Virus." Indian Journal of Science and Technology 15, no. 10 (2022): 451–56. https://doi.org/10.17485/IJST/v15i10.491.

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Abstract <strong>Objectives:</strong> To predict the structure of L-HBsAg envelope protein of Hepatitis B Virus and its evolutionary relationship. <strong>Methods:</strong> Bioinformatics Computational methods were used for the structure prediction and evolutionary conservation analysis of large envelope protein of Hepatitis B virus (L-HBsAg). Structure prediction L-HBsAg envelope protein was done using Multi-template homology modeling method using Schrodinger software. Phylogenetic tree was constructed by MEGA tool to identify protein similarity of L-HBsAg protein with other ge

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Gollan, Timothy J., and Michael R. Green. "Redirecting Retroviral Tropism by Insertion of Short, Nondisruptive Peptide Ligands into Envelope." Journal of Virology 76, no. 7 (2002): 3558–63. http://dx.doi.org/10.1128/jvi.76.7.3558-3563.2002.

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ABSTRACT A potentially powerful approach for in vivo gene delivery is to target retrovirus to specific cells through interactions between cell surface receptors and appropriately modified viral envelope proteins. Previously, relatively large (>100 residues) protein ligands to cell surface receptors have been inserted at or near the N terminus of retroviral envelope proteins. Although viral tropism could be altered, the chimeric envelope proteins lacked full activity, and coexpression of wild-type envelope was required for production of transducing virus. Here we analyze more than 40 derivat

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Zhang, Jing, Yongxiang Wang, Shuwen Fu, et al. "Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins." Viruses 13, no. 4 (2021): 613. http://dx.doi.org/10.3390/v13040613.

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Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1 mer replication construct of genotype A or D, and viral proteins were analyzed from transfecte

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Beitari, Saina, Yimeng Wang, Shan-Lu Liu, and Chen Liang. "HIV-1 Envelope Glycoprotein at the Interface of Host Restriction and Virus Evasion." Viruses 11, no. 4 (2019): 311. http://dx.doi.org/10.3390/v11040311.

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Without viral envelope proteins, viruses cannot enter cells to start infection. As the major viral proteins present on the surface of virions, viral envelope proteins are a prominent target of the host immune system in preventing and ultimately eliminating viral infection. In addition to the well-appreciated adaptive immunity that produces envelope protein-specific antibodies and T cell responses, recent studies have begun to unveil a rich layer of host innate immune mechanisms restricting viral entry. This review focuses on the exciting progress that has been made in this new direction of res

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Borisevich, Sophia S., Vladimir V. Zarubaev, Dmitriy N. Shcherbakov, Olga I. Yarovaya, and Nariman F. Salakhutdinov. "Molecular Modeling of Viral Type I Fusion Proteins: Inhibitors of Influenza Virus Hemagglutinin and the Spike Protein of Coronavirus." Viruses 15, no. 4 (2023): 902. http://dx.doi.org/10.3390/v15040902.

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The fusion of viral and cell membranes is one of the basic processes in the life cycles of viruses. A number of enveloped viruses confer fusion of the viral envelope and the cell membrane using surface viral fusion proteins. Their conformational rearrangements lead to the unification of lipid bilayers of cell membranes and viral envelopes and the formation of fusion pores through which the viral genome enters the cytoplasm of the cell. A deep understanding of all the stages of conformational transitions preceding the fusion of viral and cell membranes is necessary for the development of specif

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Wieringa, Roeland, Antoine A. F. de Vries, Martin J. B. Raamsman, and Peter J. M. Rottier. "Characterization of Two New Structural Glycoproteins, GP3 and GP4, of Equine Arteritis Virus." Journal of Virology 76, no. 21 (2002): 10829–40. http://dx.doi.org/10.1128/jvi.76.21.10829-10840.2002.

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ABSTRACT Equine arteritis virus (EAV) is an enveloped, positive-stranded RNA virus belonging to the family Arteriviridae of the order Nidovirales. Four envelope proteins have hitherto been identified in EAV particles: the predominant membrane proteins M and GL, the unglycosylated small envelope protein E, and the nonabundant membrane glycoprotein GS. In this study, we established that the products of EAV open reading frame 3 (ORF3) and ORF4 (designated GP3 and GP4, respectively) are also minor structural glycoproteins. The proteins were first characterized by various analyses after in vitro tr

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