ライフサイエンスコーパス: envelope glycoprotein

1 HSV) entry through interactions with a viral envelope glycoprotein.

2 m by which HCV masks such epitopes on its E2 envelope glycoprotein.

3 more easily produced soluble version of the envelope glycoprotein.

4 sites (epitopes) on the surface of the viral envelope glycoprotein.

5 entry via direct interaction with the gp120 envelope glycoprotein.

6 gion (MPER) of the gp41 subunit of the HIV-1 envelope glycoprotein.

7 by enveloped viruses and is mediated by the envelope glycoprotein.

8 argeting both conserved regions of the HIV-1 envelope glycoprotein.

9 epitope in the gp120 C1 region of the HIV-1 envelope glycoprotein.

10 immunosuppression mediated by the retroviral envelope glycoprotein.

11 -retroviral vectors pseudotyped with various envelope glycoproteins.

12 emerging viruses for the processing of their envelope glycoproteins.

13 infection by binding to the sugars of viral-envelope glycoproteins.

14 ween the viral fusion (F) and attachment (H) envelope glycoproteins.

15 thin the paramyxovirus family, expresses two envelope glycoproteins.

16 thogenic viruses for the processing of their envelope glycoproteins.

17 virus (MV) fusion (F) and hemagglutinin (H) envelope glycoproteins.

18 f antibody targeting the gp41 subunit of the envelope glycoproteins.

19 e alpha4beta7 binding properties of 16 HIV-1 envelope glycoproteins.

20 through active participation of Sendai viral envelope glycoproteins.

21 fford immunosuppressive activity to distinct envelope glycoproteins.

22 (MACV) and Junin virus (JUNV), bound to the envelope glycoprotein 1 (GP1) with JUNV monoclonal antib

23 e show that transgenic mice expressing HIV-1 envelope glycoprotein 120 in their central nervous syste

24 Numerous studies of the anti-HIV-1 envelope glycoprotein 41 (gp41) broadly neutralizing ant

25 s have defined the structures that the RSV F envelope glycoprotein adopts before and after virus entr

26 f the interaction between the gp120 exterior envelope glycoprotein and CD4; (ii) premature triggering

27 s target novel conserved epitopes within the envelope glycoprotein and exhibit protective efficacy in

28 D), in the transmembrane (TM) subunit of the envelope glycoprotein and identified two naturally polym

29 ction bind to conserved regions on the virus envelope glycoprotein and potently neutralize the majori

30 mutations stabilize the ground state of the envelope glycoprotein and should thus be useful in the d

31 s, a key one being that between the viral E2 envelope glycoprotein and the CD81 receptor.

32 eir host cells via interaction between their envelope glycoproteins and cell-surface glycosaminoglyca

33 minants of the binding affinity with ASLV(A) envelope glycoproteins and to mediate efficient infectio

34 the dynamic and complex nature of this viral envelope glycoprotein, and can serve as a reference for

35 ing antibody (bNAb) responses targeting E1E2 envelope glycoproteins are generated in many individuals

36 Viral envelope glycoproteins are important for viral pathogeni

37 y suggesting that at the virion surface, HCV envelope glycoproteins are not accessible for HS binding

38 The ASLV(A) envelope glycoproteins are organized into functional dom

39 HIV-1 envelope glycoproteins are targets of neutralizing antib

40 rmined by the co-receptor usage of the viral envelope glycoproteins as well as IFITM subcellular loca

41 ection, the production of antibodies against envelope glycoprotein B (gB) is delayed, compared with p

42 The envelope glycoprotein B (gB) of HCMV is a major antigen

43 The HIV-1 envelope glycoprotein binds cooperatively to its cellula

44 we demonstrate that MAbs targeting the HIV-1 envelope glycoprotein both suppress acute SHIV plasma vi

45 d to epitopes that are expressed on isolated envelope glycoproteins but not on the native envelope tr

46 f human cells is the processing of the viral envelope glycoprotein by the cellular subtilisin kexin i

47 t individual HIV-1 differs in the numbers of envelope glycoproteins by more than one order of magnitu

48 airs the normal cellular trafficking of JSRV envelope glycoproteins by sequestering them within the G

49 The fusion peptide of the envelope glycoprotein can be targeted by anchor inhibito

50 Antibody responses to the HIV-1 envelope glycoproteins can be classified into three grou

51 that a single missense mutation in the viral envelope glycoprotein complex (GPC) is responsible for a

52 427 in the fusion subunit (GP2) of the viral envelope glycoprotein complex (GPC), thereby raising con

53 gulates the composition of alternative viral envelope glycoprotein complexes raises the intriguing po

54 cell-specific receptors by one of the viral envelope glycoprotein complexes.

55 forms of CD4, CD4bs antibodies poorly induce envelope glycoprotein conformations that efficiently bin

56 deficiency virus (HIV and SIV, respectively) envelope glycoproteins contain a highly conserved, membr

57 Although isolated HCV envelope glycoproteins could interact with heparin, none

58 ed GYxxO trafficking signal in the SIVmac239 envelope glycoprotein cytoplasmic domain, producing a vi

59 trafficking motif in the viral transmembrane envelope glycoprotein cytoplasmic tail leads in pig-tail

60 Binding of herpes simplex virus 1 (HSV-1) envelope glycoprotein D (gD) to the receptor 3-O-sulfate

61 bodies fused to a receptor-binding-deficient envelope glycoprotein D (gD).

62 ing of the CD4-mimetic compound to the HIV-1 envelope glycoproteins depends upon how many of the thre

63 Here, we show that the envelope glycoprotein domain I/II hinge of DENV-3 and DE

64 neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, re

65 cine antigens for the antigenic sites of HCV envelope glycoproteins E1 (residues 314-324) and E2 (res

66 Abs that recognize the envelope glycoproteins E1 and E2 are generated during th

67 Hepatitis C virus (HCV) envelope glycoproteins E1 and E2 are important mediators

68 The HCV envelope glycoproteins E1 and E2 mediate viral entry, wi

69 sed on the partial crystal structures of the envelope glycoproteins E1 and E2.

70 The viral "spike" of HCV is formed by two envelope glycoproteins, E1 and E2, which together mediat

71 ells and membrane fusion are achieved by two envelope glycoproteins, E1 and E2.

72 ution structural information for the two HCV envelope glycoproteins, E1 and E2.

73 eviously, we demonstrated that a recombinant envelope glycoprotein (E1E2) vaccine (genotype 1a) elici

74 analyzed the interaction of apoE with viral envelope glycoprotein E2 and HCV virions by immunoprecip

75 odies showed that conformational epitopes of envelope glycoprotein E2 domains B and C were exposed af

76 noclonal antibodies (MAbs) against the CHIKV envelope glycoproteins E2 and E1.

77 ion with ChAdOx1-GnGc vaccine, encoding RVFV envelope glycoproteins, elicits high-titre RVFV-neutrali

78 Membrane fusion induced by the envelope glycoprotein enables the intracellular replicat

79 ctural polyprotein Gag and the clustering of envelope glycoprotein Env for infectivity.

80 turation process involving the clustering of envelope glycoprotein Env.

81 s starts with interactions between the viral envelope glycoprotein (Env) and cellular CD4 receptors a

82 binds avidly and cooperatively to the HIV-1 envelope glycoprotein (Env) and is more potent than the

83 Using the HIV-1 envelope glycoprotein (Env) and its interaction with rec

84 and guide them to cells expressing the HIV-1 envelope glycoprotein (Env) are a promising new weapon f

85 Advances in HIV-1 envelope glycoprotein (Env) design generate native-like

86 ody, termed 35O22, which binds a novel HIV-1 envelope glycoprotein (Env) epitope.

87 These antibodies preferentially recognize envelope glycoprotein (Env) epitopes induced upon CD4 bi

88 neutralizing Abs (bNAbs) targeting different envelope glycoprotein (Env) epitopes, to block HIV-1 tra

89 ses of the transmembrane subunit (TM) of the envelope glycoprotein (env) gene result in a different t

90 HIV-1 envelope glycoprotein (Env) glycosylation is important b

91 The envelope glycoprotein (Env) gp120/gp41 is required for H

92 Soluble forms of trimeric HIV-1 envelope glycoprotein (Env) have long been sought as imm

93 Designing an effective HIV-1 envelope glycoprotein (Env) immunogen for elicitation of

94 responses in animals when fused to an HIV-1 envelope glycoprotein (Env) immunogen.

95 Ab responses elicited by current HIV-1 envelope glycoprotein (Env) immunogens display narrow ne

96 en postulated to be a receptor for the HIV-1 envelope glycoprotein (Env) interaction with mucosal epi

97 embly and mediating the incorporation of the envelope glycoprotein (Env) into assembling particles.

98 The HIV-1 envelope glycoprotein (Env) is a trimer of gp120/gp41 he

99 The HIV envelope glycoprotein (Env) is covered in an array of ho

100 The trimeric HIV-1 envelope glycoprotein (Env) is critical for host immune

101 The HIV envelope glycoprotein (Env) is extensively modified with

102 The gp120/gp41 HIV-1 envelope glycoprotein (Env) is highly glycosylated, with

103 ditionally, the mechanism by which the HIV-1 envelope glycoprotein (Env) is recruited to the VS remai

104 ycans surrounding the N332 glycan on the HIV envelope glycoprotein (Env) is targeted by multiple broa

105 The envelope glycoprotein (Env) is the major target for HIV-

106 HIV-1 envelope glycoprotein (Env) is the sole target for broad

107 HIV's envelope glycoprotein (Env) is the sole target for neutr

108 The trimeric HIV-1 envelope glycoprotein (Env) is the sole target of virus-

109 Since the envelope glycoprotein (Env) is the target of neutralizin

110 esidues (G382R and H442Y) into the SIVmac239 envelope glycoprotein (Env) markedly increased its neutr

111 The development of soluble envelope glycoprotein (Env) mimetics displaying ordered

112 es the exposure of epitopes within the viral envelope glycoprotein (Env) on the surface of infected c

113 Structure determination of the HIV-1 envelope glycoprotein (Env) presented a number of challe

114 ies (MAbs) to distinct epitopes on the viral envelope glycoprotein (Env) provides the potential to us

115 Envelope glycoprotein (Env) reactivity (ER) describes th

116 to autologous CD4(+) T cells through a viral envelope glycoprotein (Env) receptor- and actin-dependen

117 r to other type I fusion machines, the HIV-1 envelope glycoprotein (Env) requires proteolytic activat

118 The HIV-1 envelope glycoprotein (Env) spike is the only target for

119 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike should expose as many

120 The HIV-1 envelope glycoprotein (Env) spike, located on the outsid

121 requires Ab accessibility to the functional envelope glycoprotein (Env) spike.

122 broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) spike.

123 HIV-1 envelope glycoprotein (Env) spikes are prime vaccine can

124 The trimeric envelope glycoprotein (Env) spikes on HIV-1 are known to

125 are among viruses for having a low number of envelope glycoprotein (Env) spikes per virion, i.e., app

126 re of these proteins is their mimicry of the envelope glycoprotein (Env) structure on virus particles

127 alizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) suppress viremia in animal m

128 broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sit

129 erally designed to mimic the native trimeric envelope glycoprotein (Env) that is the target of virus-

130 this insight to generate a form of SIVmac239 envelope glycoprotein (Env) that utilized rhesus CD4 mor

131 inner domain of gp120 are required for HIV-1 envelope glycoprotein (Env) transitions to the CD4-bound

132 alizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) trimer has facilitated its s

133 ibody immune evasion strategies of the HIV-1 envelope glycoprotein (Env) trimer include conformationa

134 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer maintain the metastab

135 The HIV-1 surface envelope glycoprotein (Env) trimer mediates entry into C

136 The envelope glycoprotein (Env) trimer on the surface of HIV

137 on the unliganded conformation of the HIV-1 envelope glycoprotein (Env) trimer represent barriers to

138 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, which consists of th

139 expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer.

140 Soluble envelope glycoprotein (Env) trimers (SOSIP.664 gp140) ar

141 Soluble, recombinant native-like envelope glycoprotein (Env) trimers of various human imm

142 The homotrimeric HIV-1 envelope glycoprotein (Env) undergoes receptor-triggered

143 Current HIV-1 envelope glycoprotein (Env) vaccine candidates elicit pr

144 transmitted/founder (T/F) SIVsmE660-derived envelope glycoprotein (Env) variants from 14 RMs immuniz

145 CD4) is a suboptimal receptor for most HIV-1 envelope glycoprotein (Env) variants.

146 antibodies against vulnerable regions on the envelope glycoprotein (Env) viral spike.

147 particles displaying trimeric membrane-bound envelope glycoprotein (Env) were tested in a phase 2a tr

148 Interaction of the viral envelope glycoprotein (Env) with a specific cellular rec

149 nserved coreceptor-binding site of the HIV-1 envelope glycoprotein (Env), can increase the associatio

150 t epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 an

151 immunogens that antigenically mimic the HIV envelope glycoprotein (Env), such as the soluble cleaved

152 antitatively or qualitatively modulate HIV-1 envelope glycoprotein (Env)-specific B and T cell respon

153 nizing epitopes in the V1/V2 region of HIV-1 envelope glycoprotein (Env).

154 y include a recombinant version of the viral envelope glycoprotein (Env).

155 essing and virion incorporation of the viral envelope glycoprotein (Env).

156 to the CD4 binding site (CD4bs) on the HIV-1 envelope glycoprotein (Env).

157 ng antibodies (bnAbs) that bind to the viral envelope glycoprotein (Env).

158 and shown to bind to conserved sites on the envelope glycoprotein (Env).

159 the enormous sequence diversity of the HIV-1 envelope glycoprotein (Env).

160 rstanding germline bNAb recognition of HIV-1 envelope glycoprotein (Env).

161 nization with recombinant forms of the viral envelope glycoprotein (Env; the target of anti-HIV-1 neu

162 ion of replication-competent provirus, HIV-1 envelope glycoproteins (Env) are expressed and accumulat

163 IV-1 vaccine candidates that include soluble envelope glycoproteins (Env) are tested in humans and ot

164 cytotoxicity (ADCC) requires the presence of envelope glycoproteins (Env) in the CD4-bound conformati

165 HIV-1-infected cells presenting envelope glycoproteins (Env) in the CD4-bound conformati

166 HIV-1-infected cells presenting envelope glycoproteins (Env) in the CD4-bound conformati

167 The human immunodeficiency virus (HIV-1) envelope glycoproteins (Env) mediate virus entry through

168 1) entry into cells is mediated by the viral envelope glycoproteins (Env), a trimer of three gp120 ex

169 HIV-1 and its surface envelope glycoproteins (Env), gp120 and gp41, have evolv

170 onses to the conserved elements of the HIV-1 envelope glycoproteins (Env), including the primary rece

171 ause of the genetic variability of the HIV-1 envelope glycoproteins (Env), the elicitation of neutral

172 f the virus, which is most pronounced in the envelope glycoproteins (Env), which are the sole targets

173 1 into target cells is mediated by the viral envelope glycoproteins (Env).

174 Vaccine-elicited antibodies target the viral envelope glycoproteins (Envs) and can potentially inhibi

175 The envelope glycoproteins (Envs) from human immunodeficienc

176 The envelope glycoproteins (Envs) of HIV-1 continuously evol

177 The envelope glycoproteins (Envs) on the surfaces of HIV-1 p

178 In presence of cells expressing HIV-1 envelope glycoproteins (Envs), these BiKEs activated spe

179 receptor-binding protein (HN) and the fusion envelope glycoprotein (F), which together comprise the m

180 ity of an HIV SAM vaccine encoding a clade C envelope glycoprotein formulated with a cationic nanoemu

181 ructurally resembles the gp41 subunit of the envelope glycoprotein from human immunodeficiency virus

182 HCV (HCVcc) containing patient-derived viral envelope glycoproteins from 22 HCV variants isolated fro

183 derived HCV containing patient-derived viral envelope glycoproteins from 22 HCV variants isolated fro

184 osomal compartment and is facilitated by the envelope glycoprotein fusion subunit, GP2.

185 The envelope glycoprotein (G) of VSV was replaced with a var

186 erpes simplex virus (HSV), requires the four envelope glycoproteins gB, gD, gH, and gL.

187 e, we describe the crystal structure of HTNV envelope glycoprotein Gn, an integral component of the G

188 Fusion is mediated by the EBOV envelope glycoprotein GP, which consists of subunits GP1

189 Evidence suggests that the EBOV envelope glycoprotein (GP) also counteracts BST2, althou

190 1 lentiviral vector with its homologous gp41 envelope glycoprotein (GP) cytoplasmic tail (CT), we cre

191 at the Ebola virus matrix protein, VP40, and envelope glycoprotein, GP, each cooperate with BST2 to i

192 Although the Ebola virus envelope glycoprotein (GP1,2) antagonizes the trapping o

193 d a neuropathic pain model of perineural HIV envelope glycoprotein gp120 application onto the rat sci

194 The HIV-1 envelope glycoprotein gp120 is heavily glycosylated and

195 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 is not adequately explained

196 tions, which seem to be independent of viral envelope glycoprotein gp120, are poorly understood.

197 cluding a possible contribution by the HIV-1 envelope glycoprotein gp120, which binds with high affin

198 ns via targeting the CD4 binding site of the envelope glycoprotein gp120.

199 r- and coreceptor-binding sites of the HIV-1 envelope glycoprotein gp120.

200 bind to the N-linked glycans coating the HIV envelope glycoproteins gp120 and gp41, highlighting them

201 tly located within the variable loops of the envelope glycoprotein (gp120), particularly in V1/V2.

202 rst time demonstrates a role of POX in HIV-1 envelope glycoprotein (gp120)-induced neuronal autophagy

203 e cluster of high-mannose glycans on the HIV envelope glycoprotein, gp120, are being highlighted as i

204 a direct interaction with the external viral envelope glycoprotein, gp120.

205 Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasm

206 eins after basic residues, including the HIV envelope glycoprotein (gp160) and Vpr.

207 on F427I in the transmembrane region of JUNV envelope glycoprotein GP2 has been shown to attenuate th

208 0, recognize a conserved region on the HIV-1 envelope glycoprotein gp41 adjacent to the viral membran

209 The envelope glycoprotein gp41 mediates the process of membr

210 bstitutions in the cytoplasmic tail of viral envelope glycoprotein gp41 of the neurovirulent virus SI

211 ollicles produce IgG Abs reactive with viral envelope glycoprotein gp41 trimers, and these Abs are co

212 moderately reduced trafficking of the viral envelope glycoprotein GP64 to the plasma membrane but dr

213 rus, which binds to the cell surface via the envelope glycoprotein Gp64.

214 into the host cell is promoted by the virus envelope glycoprotein GPC.

215 l membranes, a process mediated by the virus envelope glycoprotein GPC.

216 lecule inhibitors that target the arenavirus envelope glycoprotein (GPC) have recently been identifie

217 dentified and shown to act on the arenavirus envelope glycoprotein (GPC) to prevent membrane fusion.

218 Unlike other viral envelope glycoproteins, GPC contains a myristoylated sta

219 eproduces the features of AHF identified the envelope glycoproteins (GPs) as the major determinants o

220 he role played by integrins and by the viral envelope glycoprotein H in entry and cell-to-cell spread

221 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein have been studied extensively for

222 We found that the HIV-1 membrane envelope glycoproteins have a unique pattern of carbohyd

223 The envelope glycoproteins have an extensive coat of carbohy

224 virus (VSV) encoding the hemagglutinin-like envelope glycoproteins HL17 or HL18 in place of the VSV

225 We demonstrate that HIV-1 envelope glycoprotein immunization activates a highly po

226 dly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advanc

227 cryo-EM) and allowed us to stabilize the HIV envelope glycoprotein in a functional state.

228 in providing the necessary stability to the envelope glycoprotein in order to withstand the interact

229 Despite the known function of viral envelope glycoproteins in catalyzing fusion with cellula

230 res the coordinated action of multiple virus envelope glycoproteins, including gH, gL, and gB.

231 Here, we report that B virus lacking the gD envelope glycoprotein infects both human and monkey cell

232 w that oBST2B decreases the incorporation of envelope glycoprotein into JSRV viral particles, which i

233 The hepatitis C virus (HCV) E2 envelope glycoprotein is crucial for virus entry into he

234 The E2 envelope glycoprotein is the primary target of human neu

235 his study, mutations naturally found in some envelope glycoproteins lacking immunosuppressive activit

236 triggering of conformational changes in the envelope glycoproteins, leading to irreversible inactiva

237 amino acid residue at position 162 in the E2 envelope glycoprotein (lysine in SFV4, glutamic acid in

238 NiV's attachment (G) and fusion (F) envelope glycoproteins mediate viral binding to the ephr

239 inhibits HCV infection despite increased HCV envelope glycoprotein-mediated infection of liver cells.

240 additionally express the HBV middle surface envelope glycoprotein (MHBs) induces functional CD8 T ce

241 ed that the majority of substitutions in the envelope glycoproteins occurred at the E2-E2 interface.

242 E Approximately 50% of the mass of the gp120 envelope glycoprotein of both HIV and SIV is N-linked ca

243 E2, the major envelope glycoprotein of classical swine fever virus (CS

244 The envelope glycoprotein of diverse endogenous and exogenou

245 We then identified the envelope glycoprotein of EIAV as a determinant that also

246 ate the binding affinities between the gp120 envelope glycoprotein of HIV-1 and three broadly neutral

247 pped to a conserved domain of the retroviral envelope glycoprotein of several exogenous as well as en

248 hese two key residues (E14R and A20F) in the envelope glycoprotein of the Friend murine leukemia viru

249 RNA (mRNA-LNP) encoding the pre-membrane and envelope glycoproteins of a strain from the ZIKV outbrea

250 ation of the glycans on the natural membrane envelope glycoproteins of HIV-1, a carbohydrate profile

251 The trimeric envelope glycoproteins of human immunodeficiency virus t

252 oxicity (ADCC), whereby host antibodies bind envelope glycoproteins of the virus that are inserted in

253 d elicit antibodies that bind to the surface envelope glycoproteins on the membrane of the virus.

254 Since all retroviruses share an envelope glycoprotein organization, they likely share a

255 support for a vaccine comprising recombinant envelope glycoproteins, perhaps in a formulation with a

256 MeV envelope glycoproteins preassemble intracellularly into

257 enavirus life cycle, processing of the viral envelope glycoprotein precursor (GPC) by the cellular su

258 oreover, capture and transfer of Nipah virus envelope glycoprotein-pseudotyped lentivirus particles b

259 Similarly, a vaccine comprising recombinant envelope glycoproteins (rE1E2) derived from the genotype

260 d dead or dying, were taken up through viral envelope glycoprotein-receptor-independent interactions,

261 fferences in the amount of virion-associated envelope glycoprotein, recipient isolates were on averag

262 h a conserved linear epitope from the HCV E2 envelope glycoprotein (residues 412 to 423; epitope I),

263 nstrated that pseudotyping with rabies virus envelope glycoprotein (RV-G) enabled the axonal retrogra

264 We tested the ability of HIV-1 envelope glycoprotein-specific broadly neutralizing MAbs

265 The trimeric HIV-1 envelope glycoprotein spike (Env) mediates viral entry i

266 The trimeric envelope glycoprotein spike (Env) of HIV-1 is the target

267 Knowledge of the envelope glycoprotein structure and the conformational c

268 The surface envelope glycoprotein (SU) of Human immunodeficiency vir

269 tion structures of the monomeric core of the envelope glycoprotein subunit gp120 and, more recently,

270 human immunodeficiency virus, type 1 (HIV-1) envelope glycoprotein subunit gp41 is targeted by potent

271 l region and the transmembrane domain of the envelope glycoprotein subunit gp41, which display differ

272 of the few immunogenic targets on the virus envelope glycoprotein that can induce neutralizing antib

273 hat the product of the UL116 gene is an HCMV envelope glycoprotein that forms a novel gH-based comple

274 identify residues in the HIV-1 transmembrane envelope glycoprotein that stabilize the unliganded stat

275 us, where most variation occurs in the viral envelope glycoproteins that are the sole targets for neu

276 er preparations of HCV particles with tagged envelope glycoproteins that enabled ultrastructural anal

277 e studies that employ challenge strains with envelope glycoproteins that fail to exhibit neutralizati

278 n(154) glycosylation site in each of the 180 envelope glycoproteins that make up the icosahedral shel

279 The HIV-1 and HIV-2 envelope glycoproteins, the sole targets of neutralizing

280 al entry into host cells relies on two viral envelope glycoproteins: the attachment (G) and fusion (F

281 ajority of paramyxoviruses utilize two viral envelope glycoproteins: the attachment glycoprotein (G,

282 immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational cha

283 However, the relative ability of SIV envelope glycoproteins to bind or utilize these CD4 orth

284 rus (HIV) vaccines is the inability of viral envelope glycoproteins to elicit broad and potent neutra

285 mer are bound and upon the propensity of the envelope glycoproteins to undergo conformational changes

286 Here, we present our studies on the envelope glycoprotein transmembrane subunit, GP2, of the

287 The envelope glycoprotein trimer (Env) on the surface of HIV

288 sites of a single gp120 monomer of the HIV-1 envelope glycoprotein trimer and (ii) the ability of the

289 ers changes in the conformation of the HIV-1 envelope glycoprotein trimer important for virus entry.

290 The envelope glycoprotein trimer mediates HIV-1 entry into c

291 We show that a soluble recombinant HIV-1 envelope glycoprotein trimer that adopts a native confor

292 l membranes, a process mediated by the HIV-1 envelope glycoprotein trimer.

293 mponents: 1) IgG Abs reacting with the viral envelope glycoprotein trimeric gp41; 2) produced by plas

294 use of various designs of recombinant HIV-1 envelope glycoprotein trimers that mimic the structure o

295 gen design have provided soluble recombinant envelope glycoprotein trimers with near-native morpholog

296 inated action of the MV H and the fusion (F) envelope glycoprotein; upon receptor engagement by H, th

297 n of the MV hemagglutinin (H) and fusion (F) envelope glycoproteins; upon receptor engagement by H, t

298 vesicular stomatitis virus-Zaire Ebola virus envelope glycoprotein vaccine (rVSVDeltaG-ZEBOV-GP).

299 vesicular stomatitis virus-Zaire Ebola virus envelope glycoprotein vaccine (rVSVG-ZEBOV-GP) across a

300 ibodies recognizing different regions of HCV envelope glycoproteins were also used in a pulldown assa