- PDB-7dn5: The cryo-EM structure of human papillomavirus type 58 pseudovirus -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: PDB / ID: 7dn5
タイトル
The cryo-EM structure of human papillomavirus type 58 pseudovirus
要素
Major capsid protein L1
キーワード
VIRUS (ウイルス) / particles
機能・相同性
機能・相同性情報
T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / host cell nucleus / virion attachment to host cell / structural molecule activity 類似検索 - 分子機能
Major capsid L1 (late) protein, Papillomavirus / Major capsid L1 (late) superfamily, Papillomavirus / L1 (late) protein / Double-stranded DNA virus, group I, capsid 類似検索 - ドメイン・相同性
National Natural Science Foundation of China (NSFC)
U1705283
中国
引用
ジャーナル: J Virol / 年: 2021 タイトル: Structural basis for the shared neutralization mechanism of three classes of human papillomavirus type 58 antibodies with disparate modes of binding. 著者: Maozhou He / Xin Chi / Zhenghui Zha / Yunbing Li / Jie Chen / Yang Huang / Shiwen Huang / Miao Yu / Zhiping Wang / Shuo Song / Xinlin Liu / Shuangping Wei / Zekai Li / Tingting Li / Yingbin ...著者: Maozhou He / Xin Chi / Zhenghui Zha / Yunbing Li / Jie Chen / Yang Huang / Shiwen Huang / Miao Yu / Zhiping Wang / Shuo Song / Xinlin Liu / Shuangping Wei / Zekai Li / Tingting Li / Yingbin Wang / Hai Yu / Qinjian Zhao / Jun Zhang / Qingbing Zheng / Ying Gu / Shaowei Li / Ningshao Xia / 要旨: Human papillomavirus type 58 (HPV58) is associated with cervical cancer and poses a significant health burden worldwide. Although the commercial 9-valent HPV vaccine covers HPV58, the structural and ...Human papillomavirus type 58 (HPV58) is associated with cervical cancer and poses a significant health burden worldwide. Although the commercial 9-valent HPV vaccine covers HPV58, the structural and molecular-level neutralization sites of the HPV58 complete virion are not fully understood. Here, we report the high-resolution (∼3.5 Å) structure of the complete HPV58 pseudovirus (PsV58) using cryo-electron microscopy (cryo-EM). Three representative neutralizing monoclonal antibodies (nAbs 5G9, 2H3 and A4B4) were selected through clustering from a nAb panel against HPV58. Bypassing the steric hindrance and symmetry-mismatch in the HPV Fab-capsid immune-complex, we present three different neutralizing epitopes in the PsV58, and show that, despite differences in binding, these nAbs share a common neutralization mechanism. These results offer insight into HPV58 genotype specificity and broaden our understanding of HPV58 neutralization sites for antiviral research. Cervical cancer primarily results from persistent infection with high-risk types of human papillomavirus (HPV). HPV type 58 (HPV58) is an important causative agent, especially within Asia. Despite this, we still have limited data pertaining to the structural and neutralizing epitopes of HPV58, and this encumbers our in-depth understanding of the virus mode of infection. Here, we show that representative nAbs (5G9, 10B11, 2H3, 5H2 and A4B4) from three different groups share a common neutralization mechanism that appears to prohibit the virus from associating with the extracellular matrix and cell surface. Furthermore, we identify that the nAbs engage via three different binding patterns: top-center binding (5G9 and 10B11), top-fringe binding (2H3 and 5H2), and fringe binding (A4B4). Our work shows that, despite differences in the pattern in binding, nAbs against HPV58 share a common neutralization mechanism. These results provide new insight into the understanding of HPV58 infection.
#200 - 2016年8月 正二十面体型ウイルスの準対称性 (Quasisymmetry in Icosahedral Viruses) 類似性 (2)
-
集合体
登録構造単位
B: Major capsid protein L1 A: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
B: Major capsid protein L1 A: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
B: Major capsid protein L1 A: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
x 5
icosahedral pentamer
1.77 MDa, 30 ポリマー
分子量 (理論値)
分子数
合計 (水以外)
1,773,096
30
ポリマ-
1,773,096
30
非ポリマー
0
0
水
0
タイプ
名称
対称操作
数
point symmetry operation
5
4
B: Major capsid protein L1 A: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
x 6
icosahedral 23 hexamer
2.13 MDa, 36 ポリマー
分子量 (理論値)
分子数
合計 (水以外)
2,127,715
36
ポリマ-
2,127,715
36
非ポリマー
0
0
水
0
タイプ
名称
対称操作
数
point symmetry operation
6
5
登録構造と同一(異なる座標系)
icosahedral asymmetric unit, std point frame
タイプ
名称
対称操作
数
transform to point frame
1
対称性
点対称性: (シェーンフリース記号: I (正20面体型対称))
-
要素
#1: タンパク質
MajorcapsidproteinL1
分子量: 59103.199 Da / 分子数: 6 / 由来タイプ: 組換発現 由来: (組換発現) Human papillomavirus type 58 (パピローマウイルス) 遺伝子: L1 / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P26535
-
実験情報
-
実験
実験
手法: 電子顕微鏡法
EM実験
試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法
-
試料調製
構成要素
名称: Human papillomavirus type 58 / タイプ: VIRUS / Entity ID: all / 由来: RECOMBINANT
由来(天然)
生物種: Human papillomavirus type 58 (パピローマウイルス)
由来(組換発現)
生物種: Homo sapiens (ヒト)
ウイルスについての詳細
中空か: NO / エンベロープを持つか: NO / 単離: SPECIES / タイプ: VIRION