ライフサイエンスコーパス: VHH

1 VHH building blocks were assembled into highly potent ne

2 VHH heterodimer toxin-neutralizing agents containing two

3 VHH proteins recognizing foot-and-mouth disease virus (F

4 VHH sequences were modified by inclusion of a C-terminal

5 VHH single-domain antibodies have been demonstrated to n

6 VHH-based CAR T cells can thus function as antitumor age

7 is highly divergent from previous anti-HIV-1 VHH and its own germline sequence.

8 Eight of 15 VHH inhibited the cleavage of substrate SNAP25 (synaptos

9 Here, we characterized a new set of 15 VHHs against the anthrax toxins that act by binding to t

10 All 16 VHHs were suitable primary reagents for the detection of

11 For 16 VHHs, the corresponding antigens were identified by affi

12 g, named cs130-TNF(VHH)Fc and cs130-IL-12/23(VHH)Fc.

13 Crystal structures of IL-2R:VHH complexes revealed that variation in receptor dimer

14 Importantly, anti-LRP5/6 VHHs block the growth of Wnt-hypersensitive Rnf43/Znrf3-

15 A VHH to 2,4-dichlorophenoxyacetic acid (2,4-D) was used t

16 toxins can be promoted by coadministering a VHH-based toxin-neutralizing agent with an antitag monoc

17 HHs from an immunized alpaca and developed a VHH-based immunoassay using 3-phenoxybenzoic acid (3-PBA

18 extracts and more particularly to generate a VHH phage library against native Arabidopsis thaliana se

19 on of functional VHH clones, we identified a VHH-72 triple mutant (T60P.D61P.D100eY), which maintaine

20 In an exploratory experiment in mice, a VHH-PTH peptide conjugate showed biological activity, wh

21 Here we describe the construction of a VHH phage display library against the cyanobacterial hep

22 port the discovery and characterization of a VHH single domain antibody (nanobody) isolated from a ll

23 Administration of a VHH(kappa) adduct modified with 4 zanamivir molecules (V

24 ed storage protein cruciferin with that of a VHH-Fc antibody without endogenous target.

25 In this study, a VHH phagemid library generated from a llama that was mul

26 X-ray crystal structure of the BoNT/A Lc-Aa1 VHH complex at 2.6 A resolution.

27 The structure reveals that the Aa1 VHH binds in the alpha-exosite of the BoNT/A Lc, far fro

28 This variable domain of an H chain-only Ab (VHH or nanobody) significantly inhibited both phosphoant

29 r stalk region between transmembrane and AIP(VHH) in the synthetic receptors AIP2(VHH)gp130Deltastalk

30 For the synthetic receptors, AIP(VHH) were fused to the activating interleukin-6 cytokine

31 and AIP(VHH) in the synthetic receptors AIP2(VHH)gp130Deltastalk and AIP3(VHH)gp130Deltastalk to incr

32 receptors AIP2(VHH)gp130Deltastalk and AIP3(VHH)gp130Deltastalk to increase rigidity and enhanced th

33 Furthermore, several of the anti-albumin VHHs were used successfully for storage protein localisa

34 All VHHs bind the capsid in the canyon at sites that extensi

35 All VHHs were able to recognize SARS-CoV-2 in infected cells

36 olic expression of NP-specific VHHs (alphaNP-VHHs) disrupts virus replication at an early stage of th

37 Although VHH domains can function in the absence of an interloop

38 glycosylphosphatidylinositol (GPI)-anchored VHH JM2 and JM4 along with an E4 control and transduced

39 ly isolated (here referred to as VHH JM2 and VHH JM4, respectively).

40 Another VHH appears to recognize the LF C-terminal domain and ex

41 ized three single domain camelid antibodies (VHH) against cluster II.

42 e variable domain of heavy-chain antibodies (VHH) were isolated, transcribed to cDNA, and cloned into

43 loying His6-tagged single-domain antibodies (VHH).

44 ents of camelid heavy chain-only antibodies (VHH) conjugated to Pseudomonas exotoxin A to deplete mye

45 ble domains of llama heavy-chain antibodies (VHHs) as capture molecule, and a surface plasmon resonan

46 therapeutic use of single-chain antibodies (VHHs) is limited by their short half-life in the circula

47 Camelid-derived single domain antibodies (VHHs) exhibit potent antimicrobial activity and are bein

48 e the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized c

49 two llama-derived single-domain antibodies (VHHs) that have potent RSV-neutralizing activity and bin

50 ated a panel of single-VH domain antibodies (VHHs) that recognize distinct epitopes within IpaD.

51 d on llama-derived single-domain antibodies (VHHs), for the development of bunyavirus biotherapeutics

52 erapeutics such as single-domain antibodies (VHHs).

53 omains of llama heavy chain-only antibodies (VHHs) against ETEC to the Fc part of a porcine immunoglo

54 able domains of heavy-chain-only antibodies (VHHs) are becoming a salient option as immunoassay reage

55 fferent camelid heavy-chain only antibodies (VHHs) joined via peptide linkers have proven to have pot

56 ains of camelid heavy chain-only antibodies (VHHs) with affinity for PA were obtained from immunized

57 Nanobodies (single-domain antibodies, VHH) are the smallest antibody-based fragments possessin

58 chain interface of conventional antibodies, VHHs are not particularly apt to bind small analytes and

59 radiolabeled single-domain variable antibody VHH fragments (Nanobodies).

60 d in a natural camelid heavy-chain antibody (VHH) that binds to ribonuclease A.

61 Here, a single domain antibody (VHH) that binds HuR with low nanomolar affinity was iden

62 ble domain of the heavy-chain-only antibody (VHH), are single-domain antigen-binding fragments derive

63 ed from a camelid heavy-chain-only antibody (VHH).

64 ing camelid single-domain antibodyfragments (VHHs) as capture agents.

65 Antiviral VHHs prevented nuclear import of viral ribonucleoprotein

66 We identified 19 antiviral VHHs that protect human A549 cells from lethal infection

67 been recently isolated (here referred to as VHH JM2 and VHH JM4, respectively).

68 ricin-specific VHH heterodimers, as well as VHH homodimers, and characterized them for their ability

69 chips with randomly immobilized biotinylated VHHs were compared to streptavidin-coated SPR chips, on

70 similar quantities of oriented biotinylated VHHs were non-covalently immobilized.

71 chanisms by which these so-called bispecific VHH heterodimers promote toxin neutralization remain poo

72 JKH-C7 and the receptor-blocking VHH class (JIK-B8) were expressed as a heterodimeric VHH

73 re further improved by using the phage borne VHH, IC(50) = 0.1 ng/mL and LOD = 0.01 ng/mL.

74 rgets reveal two distinct epitopes, but both VHHs interfere with receptor binding.

75 alization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as usefu

76 Here, we built large dromedary camel VHH phage libraries to isolate nanobodies that broadly n

77 xposed to elevated temperatures, the camelid VHH antibodies retained more reactivity than a polyclona

78 alternates is demonstrated for three camelid VHH domain-porcine alpha-amylase interactions.

79 in complexes with four 80S-specific camelid VHHs (Nanobodies).

80 thermodynamics for an anti-caffeine camelid (VHH) antibody.

81 gen recognition and, in particular, camelid (VHH) domains.

82 Both anti-class II MHC and anti-CD11b VHHs detected inflammation with excellent specificity.

83 A (89)Zr-labeled PEGylated anti-CD8 VHH detected thymus and secondary lymphoid structures as

84 A cDNA-VHH library was constructed from a camel immunized with

85 erminal beta-strand of either a single-chain VHH antibody or a supercharged monobody, CATK-1 enabled

86 nity single variable domains on heavy chain (VHH) antibodies that bind to the periplasmic side of HiS

87 y of the variable domain of the heavy chain (VHH).

88 ct of a seed-expressed nanobody-heavy chain (VHH-Fc) antibody against the highly abundant Arabidopsis

89 Nanobody-heavy chain (VHH-Fc) antibody formats have the potential to immunomod

90 ecognizes immunoglobulin kappa light chains (VHH(kappa)) and a nanobody that recognizes either CTLA-4

91 eneration of antibody variable heavy chains (VHHs), single-chain variable fragments (scFvs) and full

92 better efficacy than the separate component VHHs.

93 ich each of the six camelid sdAb components (VHHs) can neutralize one of three different Botulinum ne

94 tion potencies compared to the corresponding VHH cocktails.

95 the sole neutralizing anti-RTB VHH to create VHH "heterodimers." As compared with equimolar concentra

96 s depends however on the capacity to deliver VHHs with optimal physico-chemical properties for their

97 Camelid-derived VHH single-domain Abs specific for human NKp30 and a hum

98 antibody fragments, such as camelid-derived VHHs, can serve as inhibitors or activators of intracell

99 oscopy confirms the binding pose of designed VHHs targeting influenza haemagglutinin and Clostridium

100 We therefore focused on developing VHH-based, single-domain antibody (nanobody) CAR T cells

101 olecules engineered to present two different VHHs fused to an Fc domain were further shown to be effe

102 reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-rea

103 tion on BoNT/A Lc yielded 15 yeast-displayed VHH with equilibrium dissociation constants (K(d)) from

104 We identified 25 distinct VHH families binding trimeric Env, of which 6 neutralize

105 a library of non-immune llama single-domain VHH (camelid heavy-chain variable region derived from he

106 aller antibody fragments, the single-domain (VHH) version of JM4 neutralized less well than the full-

107 ion of a camelid heavy-chain-only VH domain (VHH)-based neutralizing agent (VNA) targeting Stx1 and S

108 in complex with the antigen binding domains (VHH) of five unique single-chain monoclonal antibodies t

109 agged, heavy chain-only antibody VH domains (VHHs) specific for the ricin enzymatic (RTA) and binding

110 role of an additional hallmark of dromedary VHHs, i.e. the extra disulfide bond between the first an

111 nding surface on the VHHs is unique for each VHH.

112 ed anti-EGFR-iRGD consisting of an anti-EGFR VHH (the variable domain from the heavy chain of the ant

113 Further, by engineering VHHs targeting distinct, conserved epitopes into multi-v

114 r mouse and human red blood cells to express VHHs against botulinum neurotoxin A (BoNT/A) on their su

115 We expressed VHHs from an immunized alpaca and developed a VHH-based

116 e that engineered red blood cells expressing VHHs can provide prolonged prophylactic protection again

117 in vivo antibody maturation process favoring VHH domains with an interloop disulfide bond.

118 All five VHHs bind deep in the virus canyon at similar sites that

119 ound to participate in binding with all five VHHs.

120 Rather, the five VHHs had overlapping structural epitopes on the surface

121 ngly extensive) surface for each of the five VHHs.

122 e peptide (3 kDa) containing the epitope for VHH recognition was tested, much larger effects of captu

123 In this way, four VHH-IgG and four VHH-IgA antibodies were produced to levels of about 3% a

124 In this way, four VHH-IgG and four VHH-IgA antibodies were produced to lev

125 Interestingly, although the four VHHs bind to the same site, the structures of the expand

126 o identify single-domain antibody fragments (VHH) that bind the LRP6 P3E3P4E4 region with nanomolar a

127 We generated single-domain Ab fragments (VHHs) specific for class II MHC (MHCII), CD11b, and CD36

128 id-derived single-domain antibody fragments (VHHs or nanobodies) offer a possible solution to this ch

129 d to yield single-domain antibody fragments (VHHs or nanobodies) that overcome many of these shortcom

130 id-derived single-domain antibody fragments (VHHs) against influenza virus nucleoprotein (NP), a vira

131 PEGylated single-domain antibody fragments (VHHs) specific for CD8 to track the presence of intratum

132 rary of heavy chain-only antibody fragments (VHHs), we isolated an antibody (1B7) that binds TgCDPK1

133 from the resulting population of functional VHH clones, we identified a VHH-72 triple mutant (T60P.D

134 looctyne was reacted to azide functionalized VHH domains, using click chemistry.

135 GPI-VHH JM4, but not GPI-VHH JM2, in transduced CD4(+) cell

136 Finally, GPI-VHH JM4-transduced human primary CD4 T cells efficiently

137 Expression of GPI-VHH JM4, but not GPI-VHH E4 and JM2, on the surface of transduced TZM.bl cell

138 GPI-VHH JM4, but not GPI-VHH JM2, in transduced CD4(+) cell lines and human prima

139 Expression of GPI-VHH JM4, but not GPI-VHH E4 and JM2, on the surface of t

140 CR5 cells with GPI-VHH JM4, but not with GPI-VHH E4, confers resistance to both cell-free and T cell-

141 r, transduction of CEMss-CCR5 cells with GPI-VHH JM4, but not with GPI-VHH E4, confers resistance to

142 anel of heavy-chain-only antibody (Ab) V(H) (VHH) domains that neutralize Stx1 and/or Stx2 in cell-ba

143 the variable domain of heavy chain of HCAbs (VHH).

144 s (JIK-B8) were expressed as a heterodimeric VHH-based neutralizing agent (VNA2-PA).

145 ively, these data suggest that heterodimeric VHH-based neutralizing agents may function through the f

146 t-VWF interactions with a bivalent humanized VHH (caplacizumab*).

147 ies (VHH) from naive and synthetic humanized VHH phage libraries that specifically bind the S1 SARS-C

148 nction, but functional testing of identified VHHs is laborious.

149 a lentiviral screening approach to identify VHHs that elicit a phenotype when expressed intracellula

150 ructure analysis reveals that the anti-IL23R VHH employs both CDR and framework residues to achieve p

151 Structural analysis reveal that individual VHHs variably employ divergent antigen-binding regions t

152 over, structural elucidation of several IpaD-VHH complexes provided critical insights into tip comple

153 d camelid single-domain antibody (anti-PD-L1 VHH) to track PD-L1 expression by immuno-positron emissi

154 eveloped a method to site-specifically label VHHs [the variable domain (VH) of a camelid heavy-chain

155 based on the epitope predictions for leading VHHs.

156 r even single-domain antibody fragments like VHHs will be reviewed.

157 dy validates the utility of non-immune llama VHH libraries as a source of enzyme inhibitors and ident

158 en coupled to antigenic payloads, anti-MHCII VHH primed Ab responses against GFP, ubiquitin, an OVA p

159 adduct modified with 4 zanamivir molecules (VHH(kappa)-Zan(4)) was ~10-fold more potent in protectio

160 -Fcs or combination of individual monoclonal VHH-Fcs.

161 rationale for the development of multivalent VHHs that target both toxins and are broadly neutralizin

162 For clinical applications, nanobodies (VHH) derived from heavy chain only antibodies from Camel

163 idly identify and generate llama nanobodies (VHH) from naive and synthetic humanized VHH phage librar

164 wn that three anti-Marburg virus nanobodies (VHH or single-domain antibody [sdAb]) targeted a cryptot

165 hage display vector and selected nanobodies (VHHs) against native Arabidopsis seed proteins.

166 ts of PTH by conjugating them to nanobodies (VHHs) that recognize PTHR1.

167 A second neutralizing VHH (JKH-C7) recognizes a novel epitope.

168 lico modeling suggests that the neutralizing VHH binds the same residues on the Vgamma9Vdelta2 TCR as

169 ntially targeted by the broadly neutralizing VHHs as determined by competition ELISAs and 3D models o

170 structures of complexes of five neutralizing VHHs with the Mahoney strain of type 1 poliovirus at res

171 uctions of poliovirus with five neutralizing VHHs.

172 Two classes of neutralizing VHHs were identified recognizing distinct, non-overlappi

173 ents containing two linked Stx1-neutralizing VHHs or two Stx2-neutralizing VHHs were generally much m

174 1-neutralizing VHHs or two Stx2-neutralizing VHHs were generally much more potent at Stx neutralizati

175 rine macrophage assays, and the neutralizing VHHs that were tested improved survival of mice in a spo

176 consisting of two linked toxin-neutralizing VHHs, JMN-D10 and JMO-G1, was fully protective against l

177 nal assays showed that VHH(ISG15-A), but not VHH(ISG15-B), inhibits ubiquitin-specific peptidase 16-m

178 Cotransformation of VHH-IgA with the porcine joining chain and secretory com

179 sed vaccines and supports the development of VHH as anti-HIV-1 microbicides.

180 ng and aged mice immunized with two doses of VHH(MHCII)-Spike(RBD) elicit high-titer binding and neut

181 Our results demonstrate the flexibility of VHH-based CAR T cells and the potential of CAR T cells t

182 mined by competition ELISAs and 3D models of VHH-Env complexes derived from negative stain electron m

183 The crystal structure at 2.1-A resolution of VHH JM4 bound to HIV-1 YU2 gp120 stabilized in the CD4-b

184 ng demonstrates the increased versatility of VHH antibodies.

185 were obtained by promoting the isolation of VHHs with the slowest koff (off-rate selection).

186 iven the ease of manufacture and labeling of VHHs, we believe that this method could transform the ma

187 ells to prolong the circulatory half-life of VHHs.

188 ing binding site on PD-L1, with the panel of VHHs identified expected to inhibit CD80 binding.

189 ood cells by expressing chimeric proteins of VHHs with Glycophorin A or Kell.

190 Selection of VHHs recognizing BDE-47 was achieved by panning under ca

191 This set of VHHs should facilitate development of new therapeutic VN

192 cted for different nonoverlapping subsets of VHHs, allowing one to optimize the immunodetection of th

193 Recently, we reported on VHHs with in vivo activity against the protective antige

194 One VHH, L8CJ3 (J3), neutralized 96 of 100 tested HIV-1 stra

195 Of note, one VHH heterodimer could reduce Shigella hemolytic activity

196 argeted, but not antigen expression level or VHH affinity.

197 gle-domain antibody fragments (nanobodies or VHHs), to explore the dynamics and distribution of intra

198 Nanobodies, or VHHs, that recognize poliovirus type 1 have previously b

199 by comparing sensors with randomly oriented VHH (with multiple exposed azide groups) to sensors with

200 e groups) to sensors with uniformly oriented VHH (with only a single azide group).

201 The two other VHHs, E1 and V1C7, bind epitopes adjacent to V5E1 but di

202 whole-cells surface displaying an anti-3-PBA VHH as the detection element.

203 A phage VHH library was constructed, and seven VHH clones were s

204 The most potent VHH (Aa1) had a solution K(d) for BoNT/A Lc of 1.47 x 10

205 Here we present VHHs against botulinum neurotoxin A (BoNT/A) on the surf

206 The presented VHH-based technology holds great promise for the develop

207 Radiolabeled VHHs rapidly cleared the circulation (t1/2 approximately

208 2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bi

209 The cross-reactive VHHs block binding of EF/LF to the protective antigen C-

210 ght gain compared with the piglets receiving VHH-IgG producing (dose 80 mg/d per pig) or wild-type se

211 ity were compared using the FMDV-recognizing VHH.

212 nes, producing varying levels of recombinant VHH or single-chain Fv antibody fragments fused to the h

213 inate current assay development, recombinant VHHs have a high potential as alternative reagents for t

214 The variable regions (VHH) in these heavy chain-only Abs demonstrate comparabl

215 The variable regions (VHHs) of two heavy chain-only antibodies, JM2 and JM4, f

216 we developed GPI-anchored variable regions (VHHs) of two heavy chain-only antibodies, JM2 and JM4, f

217 ved crystal structures of two representative VHHs in complex with PD-L1, which revealed unique bindin

218 ide spacer to the sole neutralizing anti-RTB VHH to create VHH "heterodimers." As compared with equim

219 ntary neutralization pattern of two selected VHHs in combination covers 19 out of 21 HIV-1 strains fr

220 conclusion, a highly specific and sensitive VHH for 3-PBA was developed using sequences from immuniz

221 phage VHH library was constructed, and seven VHH clones were selected by competitive binding with 3-P

222 After phage display selection, seven VHHs recognizing the full N protein were identified by E

223 acids, we selected and characterized several VHHs that retain antigen binding capacity.

224 nking the VHHs with a GPI attachment signal, VHHs are targeted to the lipid rafts of the plasma membr

225 nking the VHHs with a GPI attachment signal, VHHs are targeted to the lipid rafts of the plasma membr

226 pite similar binding of Ly-6C/Ly-6G-specific VHH immunotoxin to granulocytes and monocytes, granulocy

227 udovirus neutralization than the bi-specific VHH-Fcs or combination of individual monoclonal VHH-Fcs.

228 ecific VHH, and one Stx1/Stx2 cross-specific VHH--was effective in preventing all symptoms of intoxic

229 ter-aided design to construct multi-specific VHH antibodies fused to human IgG1 Fc domains based on t

230 produced a new collection of ricin-specific VHH heterodimers, as well as VHH homodimers, and charact

231 receptor for current stoichiometric-specific VHH nanobodies.

232 e-tagged VHH heterotrimer--one Stx1-specific VHH, one Stx2-specific VHH, and one Stx1/Stx2 cross-spec

233 er--one Stx1-specific VHH, one Stx2-specific VHH, and one Stx1/Stx2 cross-specific VHH--was effective

234 The resulting tri-specific VHH-Fc antibodies show more potent S1 binding, S1/ACE2 b

235 he facile identification of antigen-specific VHHs and their beneficial biochemical and economic prope

236 These prefusion F-specific VHHs represent promising antiviral agents against RSV.

237 to isolate a diverse panel of NKp30-specific VHHs against different epitopes on NKp30.

238 Cytosolic expression of NP-specific VHHs (alphaNP-VHHs) disrupts virus replication at an ear

239 Among the 20 unique ricin-specific VHHs we identified, six had toxin-neutralizing activity:

240 Three neutralizing RTA-specific VHHs were each linked via a short peptide spacer to the

241 ralizing agent consisting of a double-tagged VHH heterotrimer--one Stx1-specific VHH, one Stx2-specif

242 olution structure of the influenza-targeting VHH confirms atomic accuracy of the designed complementa

243 The neutralizing Vgamma9Vdelta2 TCR VHH identified in this study might provide a novel appro

244 n protection against infection with IAV than VHH(kappa)-Zan carrying only a single zanamivir molecule

245 Thus, we conclude that VHH JM4, when targeted to the lipid rafts of the plasma

246 Functional assays showed that VHH(ISG15-A), but not VHH(ISG15-B), inhibits ubiquitin-s

247 The VHH harbors remarkable amino acid substitutions in the f

248 The VHH heterodimers did differ from the homodimers in their

249 the purple-blue amilCP chromoprotein and the VHH expression level was reduced to obtain a limit of de

250 onstant domain and a reshaped surface at the VHH side, which normally associates with L chains in con

251 emonstrated that the interaction between the VHH protein and excipients involves hydrophilic interact

252 RTA interactions were influenced most by the VHH CDR3 (CDR, complementarity-determining region) eleme

253 ly the piglets receiving feed containing the VHH-IgA-based antibodies (dose 20 mg/d per pig) were pro

254 consists of one antigen-binding domain, the VHH, and two constant domains.

255 iosensors, and azides were introduced in the VHH to function as bioorthogonal reactive groups.

256 Moreover, the VHH heterodimers that were most effective at promoting r

257 Ala scanning of the VHH revealed only three "hot spot" side chains and addit

258 The versatility of the VHH scaffold and sortase-mediated covalent attachment of

259 properties of GO with the versatility of the VHH scaffold in the context of a flow system provides a

260 rthermore, protein stability analysis of the VHH-Fcs shows favorable developability features, which e

261 Piglets receiving the VHH-IgA-based antibodies in the feed showed a progressiv

262 and applicability, strongly suggest that the VHH antibody format will play a more prominent role in f

263 We demonstrate that the VHH heterodimers, but not homodimers were able to comple

264 philic, hence more soluble, character to the VHH but decrease the intrinsic stability of the domain.

265 In addition, the VHHs prevent RSV replication and lung infiltration of in

266 In all four complexes, the VHHs bind to a site on the top surface of the capsid pro

267 We report that by genetically linking the VHHs with a GPI attachment signal, VHHs are targeted to

268 We show that by genetically linking the VHHs with a GPI attachment signal, VHHs are targeted to

269 The neutralizing mechanisms of the VHHs and their potential use as quality control agents f

270 None of the VHHs made direct contact with residues involved in RTA's

271 A subset of the VHHs neutralized against EF and/or LF in murine macropha

272 Interestingly, binding of one of the VHHs, PVSS21E, resulted in significant changes of the ca

273 The binding surfaces on the VHHs are surprisingly extensive, but despite the use of

274 ces on the virus, the binding surface on the VHHs is unique for each VHH.

275 by camelids, however the structure of their VHH regions can be readily reproduced in industrial expr

276 These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped vir

277 These VHHs recognized the in situ tip complex and modulated th

278 Six of these VHHs are cross-reactive against both EF and LF and recog

279 Crystal structures of these VHHs bound to their respective viral targets reveal two

280 Crystal structures of these VHHs in complex with prefusion F show that they recogniz

281 best immunoassay developed with one of these VHHs showed an IC(50) of 1.4 ng/mL (limit of detection (

282 One of these VHHs, V5E1, ranks as one of the most potent ricin-neutra

283 Based on their specificity, these VHHs fall into two distinct groups.

284 We show that these VHHs can target NP in living cells and perturb NP's func

285 The use of this VHH antibody reagent immobilized onto a Au electrode for

286 ciated with cell entry, suggesting that this VHH traps the virus in a previously undescribed early in

287 ir respective monovalent monomers, all three VHH heterodimers had higher affinities for ricin and, in

288 -ray crystal structures of each of the three VHHs (E1, V1C7, and V5E1) in complex with RTA.

289 Thus, VHH-mediated targeting of LRP5/6 provides a promising di

290 NF or IL-12/IL-23 signaling, named cs130-TNF(VHH)Fc and cs130-IL-12/23(VHH)Fc.

291 negative-sense RNA viruses are vulnerable to VHHs uniquely specific for their respective nucleoprotei

292 rved in which the final complex includes two VHH domains for every caffeine molecule.

293 tag present at two sites on each of the two VHH heterodimer molecules that bind to each toxin molecu

294 Two VHHs were tested in this study: one recognizing foot-and

295 We used VHHs to explore the possibility of imaging inflammation

296 We tested T cell activation using VHHs that target distinct APC populations; anti-MHCII ad

297 antibody composed of 2 heavy-chain-only VH (VHH) binding domains against both TcdA and TcdB (designa

298 izing unique structures of expanded virions, VHH binding permitted a more detailed view of the virus

299 Finally, a bispecific VNA (VHH-based neutralizing agent) consisting of two linked t

300 BDs from SARS-CoV-2 and Delta relative to WT VHH-72.