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1 epitope in the gp120 C1 region of the HIV-1 envelope glycoprotein.
2 HSV) entry through interactions with a viral envelope glycoprotein.
3 vity of SERINC5 with remodeling of the HIV-1 envelope glycoprotein.
4 immunosuppression mediated by the retroviral envelope glycoprotein.
5 lizing Abs specific for the V2 region of the envelope glycoprotein.
6 m by which HCV masks such epitopes on its E2 envelope glycoprotein.
7 more easily produced soluble version of the envelope glycoprotein.
8 xosome mimicry mechanism does not require an envelope glycoprotein.
9 antigenic site within domain II of the viral envelope glycoprotein.
10 nt the membrane-proximal region of the HIV-1 envelope glycoprotein.
11 lizing antibodies by HIV-1 vaccines based on envelope glycoproteins.
12 through active participation of Sendai viral envelope glycoproteins.
13 fford immunosuppressive activity to distinct envelope glycoproteins.
14 -retroviral vectors pseudotyped with various envelope glycoproteins.
15 emerging viruses for the processing of their envelope glycoproteins.
16 in multiple respects from the natural HIV-1 envelope glycoproteins.
17 (MACV) and Junin virus (JUNV), bound to the envelope glycoprotein 1 (GP1) with JUNV monoclonal antib
18 e show that transgenic mice expressing HIV-1 envelope glycoprotein 120 in their central nervous syste
21 f the interaction between the gp120 exterior envelope glycoprotein and CD4; (ii) premature triggering
22 s target novel conserved epitopes within the envelope glycoprotein and exhibit protective efficacy in
23 D), in the transmembrane (TM) subunit of the envelope glycoprotein and identified two naturally polym
24 ction bind to conserved regions on the virus envelope glycoprotein and potently neutralize the majori
25 mutations stabilize the ground state of the envelope glycoprotein and should thus be useful in the d
27 eir host cells via interaction between their envelope glycoproteins and cell-surface glycosaminoglyca
28 the dynamic and complex nature of this viral envelope glycoprotein, and can serve as a reference for
29 enipavirus The attachment (G) and fusion (F) envelope glycoproteins are both required for viral entry
30 ing antibody (bNAb) responses targeting E1E2 envelope glycoproteins are generated in many individuals
32 y suggesting that at the virion surface, HCV envelope glycoproteins are not accessible for HS binding
34 rmined by the co-receptor usage of the viral envelope glycoproteins as well as IFITM subcellular loca
35 ection, the production of antibodies against envelope glycoprotein B (gB) is delayed, compared with p
36 ction against HCMV infection, and the virion envelope glycoprotein B (gB) serves as a major target of
37 Ebola, influenza and numerous other viruses, envelope glycoproteins bind the infecting virion to cell
38 f human cells is the processing of the viral envelope glycoprotein by the cellular subtilisin kexin i
39 airs the normal cellular trafficking of JSRV envelope glycoproteins by sequestering them within the G
41 of concept that rational engineering of HCV envelope glycoproteins can be used to modulate E2 antige
42 that a single missense mutation in the viral envelope glycoprotein complex (GPC) is responsible for a
43 427 in the fusion subunit (GP2) of the viral envelope glycoprotein complex (GPC), thereby raising con
46 forms of CD4, CD4bs antibodies poorly induce envelope glycoprotein conformations that efficiently bin
47 deficiency virus (HIV and SIV, respectively) envelope glycoproteins contain a highly conserved, membr
51 ing of the CD4-mimetic compound to the HIV-1 envelope glycoproteins depends upon how many of the thre
52 esent evidence that these stabilized soluble envelope glycoproteins differ in multiple respects from
53 fic mutations in the CT of a gammaretroviral envelope glycoprotein distinctly affect infectivity of t
54 neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, re
58 The viral "spike" of HCV is formed by two envelope glycoproteins, E1 and E2, which together mediat
59 eviously, we demonstrated that a recombinant envelope glycoprotein (E1E2) vaccine (genotype 1a) elici
60 analyzed the interaction of apoE with viral envelope glycoprotein E2 and HCV virions by immunoprecip
61 odies showed that conformational epitopes of envelope glycoprotein E2 domains B and C were exposed af
62 s (NAbs) through molecular features of viral envelope glycoprotein E2, including hypervariable region
63 ed on structures of antibodies targeting HCV envelope glycoprotein E2, we designed immunogens to modu
64 ion with ChAdOx1-GnGc vaccine, encoding RVFV envelope glycoproteins, elicits high-titre RVFV-neutrali
65 , Ebola, Lassa or vesicular stomatitis virus envelope glycoproteins enabled us to study entry of viru
70 s starts with interactions between the viral envelope glycoprotein (Env) and cellular CD4 receptors a
71 1 enters cells through binding between viral envelope glycoprotein (Env) and cellular receptors to in
72 binds avidly and cooperatively to the HIV-1 envelope glycoprotein (Env) and is more potent than the
74 HIV-1 entry into cells is mediated by the envelope glycoprotein (Env) and represents an attractive
75 and guide them to cells expressing the HIV-1 envelope glycoprotein (Env) are a promising new weapon f
76 ane-proximal external region (MPER) of HIV-1 envelope glycoprotein (Env) can be targeted by neutraliz
81 of the human immunodeficiency virus (HIV)-1 envelope glycoprotein (Env) gp41 subunit plays a critica
82 izing antibodies (bNAbs) targeting the HIV-1 envelope glycoprotein (Env) have been shown to protect n
84 izing antibodies (bNAbs) targeting the HIV-1 envelope glycoprotein (Env) have promising utility in pr
86 ive studies with subtype A BG505-derived HIV envelope glycoprotein (Env) immunogens have revealed tha
88 embly and mediating the incorporation of the envelope glycoprotein (Env) into assembling particles.
95 ditionally, the mechanism by which the HIV-1 envelope glycoprotein (Env) is recruited to the VS remai
97 ycans surrounding the N332 glycan on the HIV envelope glycoprotein (Env) is targeted by multiple broa
101 , viral escape through mutation of the HIV-1 envelope glycoprotein (Env) limits clinical applications
102 esidues (G382R and H442Y) into the SIVmac239 envelope glycoprotein (Env) markedly increased its neutr
104 Binding of the gp120 surface subunit of the envelope glycoprotein (Env) of HIV-1 to CD4 and chemokin
105 nformation of HIV-1 Env.IMPORTANCE The HIV-1 envelope glycoprotein (Env) opens in response to recepto
107 ies (MAbs) to distinct epitopes on the viral envelope glycoprotein (Env) provides the potential to us
108 r to other type I fusion machines, the HIV-1 envelope glycoprotein (Env) requires proteolytic activat
109 We describe a new recombinant native-like envelope glycoprotein (Env) SOSIP trimer, termed AMC009,
110 entation to the immune system.IMPORTANCE The envelope glycoprotein (Env) spike on the surface of huma
114 t efforts to optimize its utility.IMPORTANCE Envelope glycoprotein (Env) spikes on the surface of hum
115 are among viruses for having a low number of envelope glycoprotein (Env) spikes per virion, i.e., app
116 re of these proteins is their mimicry of the envelope glycoprotein (Env) structure on virus particles
117 alizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) suppress viremia in animal m
119 this insight to generate a form of SIVmac239 envelope glycoprotein (Env) that utilized rhesus CD4 mor
120 inner domain of gp120 are required for HIV-1 envelope glycoprotein (Env) transitions to the CD4-bound
121 s type 1 (HIV-1) entry into cells, the viral envelope glycoprotein (Env) trimer [(gp120/gp41)(3)] bin
123 alizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) trimer has facilitated its s
124 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer maintain the metastab
127 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer of gp120-gp41 heterod
129 alizing antibodies (bNAbs) against the HIV-1 envelope glycoprotein (Env) trimer remains a major vacci
130 riggers serial conformational changes in the envelope glycoprotein (Env) trimer that result in the fu
131 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, (gp120/gp41)(3) Solu
133 1) entry into cells is mediated by the viral envelope glycoprotein (Env) trimer, which consists of th
137 he immunogenicity of native-like recombinant envelope glycoprotein (Env) trimers based on viral seque
144 nserved coreceptor-binding site of the HIV-1 envelope glycoprotein (Env), can increase the associatio
145 t epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 an
146 dense array of N-linked glycans on the HIV-1 envelope glycoprotein (Env), known as the "glycan shield
147 immunogens that antigenically mimic the HIV envelope glycoprotein (Env), such as the soluble cleaved
149 antitatively or qualitatively modulate HIV-1 envelope glycoprotein (Env)-specific B and T cell respon
150 ross-reactive antibodies that mediated HIV-1 envelope glycoprotein (Env)-targeted ADCC were frequentl
163 ion of replication-competent provirus, HIV-1 envelope glycoproteins (Env) are expressed and accumulat
165 cytotoxicity (ADCC) requires the presence of envelope glycoproteins (Env) in the CD4-bound conformati
166 The human immunodeficiency virus (HIV-1) envelope glycoproteins (Env) mediate virus entry through
167 eral strategies to limit the exposure of its envelope glycoproteins (Env) on the surface of infected
170 1) entry into cells is mediated by the viral envelope glycoproteins (Env), a trimer of three gp120 ex
172 onses to the conserved elements of the HIV-1 envelope glycoproteins (Env), including the primary rece
173 ause of the genetic variability of the HIV-1 envelope glycoproteins (Env), the elicitation of neutral
176 Our phase I study with recombinant HCV E1/E2 envelope glycoprotein (EnvGPs) as a candidate vaccine di
177 Vaccine-elicited antibodies target the viral envelope glycoproteins (Envs) and can potentially inhibi
184 ata suggest that HSV-1 gC protects the viral envelope glycoproteins essential for entry, including gB
185 ate receptors as targets for fusion with HIV envelope glycoprotein-expressing pseudovirus particles w
186 derived HCV containing patient-derived viral envelope glycoproteins from 22 HCV variants isolated fro
187 HCV (HCVcc) containing patient-derived viral envelope glycoproteins from 22 HCV variants isolated fro
188 (M) segment of the viral genome encodes two envelope glycoproteins, G(N) and G(C), which together fo
190 e, we describe the crystal structure of HTNV envelope glycoprotein Gn, an integral component of the G
194 ane proximal external region (MPER) of HIV-1 envelope glycoprotein (gp) 41 is an attractive vaccine t
196 ovalent vaccines, which all utilize the sole envelope glycoprotein (GP), do not protect against heter
197 at the Ebola virus matrix protein, VP40, and envelope glycoprotein, GP, each cooperate with BST2 to i
199 d a neuropathic pain model of perineural HIV envelope glycoprotein gp120 application onto the rat sci
204 rst time demonstrates a role of POX in HIV-1 envelope glycoprotein (gp120)-induced neuronal autophagy
205 Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasm
206 on F427I in the transmembrane region of JUNV envelope glycoprotein GP2 has been shown to attenuate th
207 bstitutions in the cytoplasmic tail of viral envelope glycoprotein gp41 of the neurovirulent virus SI
209 moderately reduced trafficking of the viral envelope glycoprotein GP64 to the plasma membrane but dr
211 Overproduction of non-ecotropic ERV (NEERV) envelope glycoprotein gp70 and resultant nephritis occur
214 lecule inhibitors that target the arenavirus envelope glycoprotein (GPC) have recently been identifie
215 dentified and shown to act on the arenavirus envelope glycoprotein (GPC) to prevent membrane fusion.
218 his importance of structural dynamics of HCV envelope glycoproteins has critical implications for vac
219 human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein have been studied extensively for
222 virus (VSV) encoding the hemagglutinin-like envelope glycoproteins HL17 or HL18 in place of the VSV
224 dly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advanc
226 in providing the necessary stability to the envelope glycoprotein in order to withstand the interact
231 Here, we report that B virus lacking the gD envelope glycoprotein infects both human and monkey cell
234 zation through structure-based design of the envelope glycoproteins is a promising route to an effect
235 E The "open" CD4-bound conformation of HIV-1 envelope glycoproteins is the primary target of antibody
236 his study, mutations naturally found in some envelope glycoproteins lacking immunosuppressive activit
237 triggering of conformational changes in the envelope glycoproteins, leading to irreversible inactiva
238 read, deep-sequenced data of full-length HCV envelope glycoprotein, longitudinally sampled from acute
239 inhibits HCV infection despite increased HCV envelope glycoprotein-mediated infection of liver cells.
242 additionally express the HBV middle surface envelope glycoprotein (MHBs) induces functional CD8 T ce
243 E Approximately 50% of the mass of the gp120 envelope glycoprotein of both HIV and SIV is N-linked ca
248 ate the binding affinities between the gp120 envelope glycoprotein of HIV-1 and three broadly neutral
249 pped to a conserved domain of the retroviral envelope glycoprotein of several exogenous as well as en
250 hese two key residues (E14R and A20F) in the envelope glycoprotein of the Friend murine leukemia viru
251 assay to detect antibodies reactive with the envelope glycoprotein of viruses in the genus Henipaviru
252 RNA (mRNA-LNP) encoding the pre-membrane and envelope glycoproteins of a strain from the ZIKV outbrea
254 d elicit antibodies that bind to the surface envelope glycoproteins on the membrane of the virus.
257 es, our results can guide the improvement of envelope glycoprotein preparations to achieve greater si
258 fferences in the amount of virion-associated envelope glycoprotein, recipient isolates were on averag
260 h a conserved linear epitope from the HCV E2 envelope glycoprotein (residues 412 to 423; epitope I),
261 HIV-1 vaccine research, native-like, soluble envelope glycoprotein SOSIP trimers are widely used for
264 isolated B cells specific for the SARS-CoV-2 envelope glycoprotein spike (S) from a COVID-19-infected
265 tigenic mammalian oligomannoses on the HIV-1 envelope glycoprotein spike that are targets for broadly
266 s to achieve greater similarity to the viral envelope glycoprotein spike, potentially increasing thei
267 the native HIV-1 Env trimer.IMPORTANCE HIV-1 envelope glycoprotein spikes mediate the entry of the vi
268 es.IMPORTANCE Engineered SOSIP trimers mimic envelope-glycoprotein spikes, which stud the surface of
270 re of these proteins is their mimicry of the envelope glycoprotein structure on virus particles that
272 l region and the transmembrane domain of the envelope glycoprotein subunit gp41, which display differ
273 hat the product of the UL116 gene is an HCMV envelope glycoprotein that forms a novel gH-based comple
274 lizing monoclonal antibodies against the SIV envelope glycoprotein that only block alpha(4)beta(7) bi
275 identify residues in the HIV-1 transmembrane envelope glycoprotein that stabilize the unliganded stat
277 er preparations of HCV particles with tagged envelope glycoproteins that enabled ultrastructural anal
278 n(154) glycosylation site in each of the 180 envelope glycoproteins that make up the icosahedral shel
279 al entry into host cells relies on two viral envelope glycoproteins: the attachment (G) and fusion (F
280 ajority of paramyxoviruses utilize two viral envelope glycoproteins: the attachment glycoprotein (G,
281 immunodeficiency virus (SIV) gp120 exterior envelope glycoprotein to CD4 triggers conformational cha
282 sed design of several epitopes of the HCV E2 envelope glycoprotein to engineer its antigenic properti
283 mportance of antibodies targeting the HCV E2 envelope glycoprotein to facilitate viral clearance.
285 rus (HIV) vaccines is the inability of viral envelope glycoproteins to elicit broad and potent neutra
286 mer are bound and upon the propensity of the envelope glycoproteins to undergo conformational changes
289 ers changes in the conformation of the HIV-1 envelope glycoprotein trimer important for virus entry.
290 We show that a soluble recombinant HIV-1 envelope glycoprotein trimer that adopts a native confor
292 mponents: 1) IgG Abs reacting with the viral envelope glycoprotein trimeric gp41; 2) produced by plas
293 use of various designs of recombinant HIV-1 envelope glycoprotein trimers that mimic the structure o
294 n of the MV hemagglutinin (H) and fusion (F) envelope glycoproteins; upon receptor engagement by H, t
295 vesicular stomatitis virus-Zaire Ebola virus envelope glycoprotein vaccine (rVSVDeltaG-ZEBOV-GP).
296 vesicular stomatitis virus-Zaire Ebola virus envelope glycoprotein vaccine (rVSVDeltaG-ZEBOV-GP).
297 vesicular stomatitis virus-Zaire Ebola virus envelope glycoprotein vaccine (rVSVG-ZEBOV-GP) across a
298 yment of the rVSVDeltaG-ZEBOV-GP Ebola virus envelope glycoprotein vaccine, available therapeutics, a
299 ibodies recognizing different regions of HCV envelope glycoproteins were also used in a pulldown assa
300 enic NDV strain, in which the ectodomains of envelope glycoproteins were replaced with the correspond