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1 I loops in three adjacent A subunits in each penton.
2 has been reported to connect the CVSC to the penton.
3 he CVSC density region that is distal to the penton.
4 cts the triplex that is one removed from the penton.
5 27 of UL25 contact the hexon adjacent to the penton.
6 ontact with the triplex one removed from the penton.
7 psid protein subunits of the hexons, not the pentons.
8 ch major capsid protein in hexons but not in pentons.
9 65, binds around the tips of both hexons and pentons.
10 tes with conformational differences in their pentons.
11 o determine the structure of capsids lacking pentons.
12 psids revealed a capsid shell composed of 12 pentons, 150 hexons, and 320 triplexes arranged on a T=1
14 and blood coagulation factor X (FX), whilst penton-alpha(v)integrin interactions are thought to cont
16 The two procapsids consist of very similar penton and hexon clusters, except for an increased curva
18 two of these proteins, VP5 (which forms the pentons and hexons in typical HSV capsids) and VP19C (a
19 of such horn-shaped densities from both the pentons and hexons of the KSHV capsid reconstructions.
24 Furthermore, these capsids also have lost pentons and peripentonal triplexes as visualized by cryo
28 ontacted both fivefold symmetrical vertices (pentons) and sixfold symmetrical faces (hexons) of the n
29 major adenovirus (Ad) capsid proteins hexon, penton, and fiber influence the efficiency and tropism o
30 by using electron cryomicroscopy, as well as penton- and protein VI-specific antibodies, we show that
31 Differential formations of the hexon and penton are mediated by a drastic alpha-helix-to-beta-str
35 ming the capsid floor between the hexons and pentons, are each composed of one molecule of ORF62 and
36 ies reveal preferential binding of ChAdOx1's penton arginine-glycine-aspartic acid (RGD) motif to the
37 eveals the free intermediate conformation of penton arms, supporting our model for coordinated moveme
42 by excess amounts of viral capsid proteins, penton base and fiber during viral replication, can trig
43 ing HAdV induces the complete release of the penton base and fiber proteins as well as a substantial
44 virus chimera, interact with HD5, bridge the penton base and fiber proteins, and provides significant
45 ins (IIIa, VIII, and IX), extensions of the (penton base and hexon) major capsid proteins, and intera
47 o reveals an altered association between the penton base and the trimeric fiber protein, perhaps refl
48 a hydrophobic ring on the top surface of the penton base and three flexible tails inserted into three
49 etween the trimeric fiber and the pentameric penton base are mediated by a hydrophobic ring on the to
50 hich retains the ability to recognize the Ad penton base as well as vitronectin, an Arg Gly Asp (RGD)
53 and its mode of attachment to the pentameric penton base by using an integrative approach of multi-re
54 eptor (CAR) at the cell surface, followed by penton base capsid protein binding to alpha(v) integrins
55 was to detarget Adv uptake through fiber and penton base capsid protein manipulations and determine h
56 d knob with lacrimal acini revealed that the penton base capsid protein remained surface associated,
64 ckievirus-and-adenovirus receptor (CAR), and penton base facilitates viral internalization by binding
65 nstrated that recombination sites within the penton base gene frame the coding sequences for the two
69 could induce a conformational change in the penton base involving clockwise untwisting of the pentam
74 virus binding could be blocked by a soluble penton base or by a function-blocking monoclonal antibod
76 pproximately 60 A) of the RGD protrusions on penton base precludes integrin binding in the same orien
77 l arrangement of five RGD protrusions on the penton base promotes integrin clustering and the signali
81 -Gly-Asp (RGD) sequence usually found in the penton base protein is important for the interaction of
84 c cells is facilitated by interaction of the penton base protein with members of the beta2 integrin f
90 ry attachment receptor, it is known that the penton base RGD motifs interact with cellular integrins
91 promoted by the binding of integrins to the penton base RGD sequence, these results suggest that vir
92 t of these novel adenoviruses indicates that penton base RGE mutation in combination with FX binding-
93 ed the interactions between the adenovirus 9 penton base subunit and alphaVbeta3 integrin using fluor
97 elate with the requirement of the pentameric penton base to simultaneously bind several integrins to
101 n serve as an alternative to the fiber knob, penton base, and hexon proteins for incorporation of tar
105 ation of the interactions of recombinant Ad5 penton base, fiber, and knob with lacrimal acini reveale
106 addition to the three major capsid proteins (penton base, hexon and fiber) and several proteins assoc
108 revealed that Ad5, fiber, and knob, but not penton base, stimulated macropinocytosis in acini and th
109 D) alphaV integrin recognition site from its penton base, was achieved in CAR-sufficient, but not CAR
130 The portal vertex appears different from pentons, being located partially inside the capsid shell
131 n be divided into three prominent regions: a penton-binding globular region, a helix-bundle stalk reg
135 eins in regulating DNA transport through the penton channel and binding to cellular transport protein
144 on the capacity of HAdV3 to produce subviral penton-dodecahedral particles that act as decoys for HD5
145 s usual sites on hexons but does not bind to pentons, even when available in 100-fold molar excess.
150 s in the three distinct morphological units: penton, hexon, and triplex of this T = 16 icosahedral pa
153 ciated tegument complexes (CATC): SCPs crown pentons/hexons and mediate tegument protein binding, and
154 the virus fiber (site of host cell binding), penton (host cell internalization signal), hexon (princi
155 internal protein VI is required to stabilize pentons in the particle while coinciding with penton rel
156 s bound to the tips of the hexons but not to pentons, indicating that KSHV SCP is attached to the upp
157 e step of virus infection and indicates that penton-integrin interactions are involved in internaliza
161 d stability, and especially the retention of pentons, is regulated by the formation of disulfide bond
164 the in vivo expanded capsid except that the pentons, normally present at the icosahedral fivefold po
166 ibody binds only to the pentameric clusters (pentons) of A subunits of the T=3 quasisymmetric virus a
168 f the major capsid protein, 60 copies of the penton protein and 1800 minor capsid proteins of which t
170 a dose of 38 mJ/cm(2) reduced the hexon and penton protein quantities to approximately 33% and 31% o
172 and prediction, we elucidated ORF142 as the penton protein, which plugs the 12 vertices of the capsi
173 minor capsid protein of Bam35 and P24 is the penton protein, with the latter finding also being suppo
175 eatment of capsids, our study indicates that penton release may be a common trend among double-strand
176 entons in the particle while coinciding with penton release upon entry and that release of protein VI
177 y, pseudotyping with the HAdV-5 fiber and/or penton RGD loop had little to no effect on in vivo trans
179 This study also demonstrates the role of penton RGD motifs in facilitating the endosome escape st
181 UL25 dimer in alphaherpesviruses, binds each penton subunit, an observation that correlates with conf
182 eak density that extends the CVSC toward the penton, suggesting either that this extra density is for
183 60 capsomers are hexons, while the rest are pentons that are correctly positioned during assembly.
185 rowding of the subunits at the centre of the pentons, thereby favouring the hexon configuration durin
187 s, with five tegument densities capping each penton vertex, a pattern highly similar to that in alpha
188 ly stabilize the hexon shell, thus rendering penton vertices the weakest links of the adenovirus caps
192 er except around the bases of the hexons and pentons, whereas they are tightly clustered into capsome
193 density as the region that is distal to the penton with the N-terminus of UL25 making contact with t