b0hzcvs

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?:abstract	The recent outbreaks and rapid international spread of SARS-CoV-2 pose a global health emergency. Its trimeric spike (S) glycoprotein interacts with human ACE2-receptor to mediate viral entry into host-cells. Here we present cryo-EM structures of a tightly closed SARS-CoV-2 S-trimer with packed fusion peptide, and an ACE2-bound S-trimer at 2.7 Å and 3.8 Å resolution, respectively. Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing-motions within the S-trimer. Noteworthy, SARS-CoV-2 S-trimer appears much more sensitive to ACE2-receptor than SARS-CoV S-trimer regarding receptor-triggered transformation from the closed prefusion state to fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2. We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2. Our findings depict the mechanism of ACE2-induced S-trimer conformational transitions from ground prefusion state toward postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics. The recent outbreaks of SARS-CoV-2 pose a global health emergency The SARS-CoV-2 trimeric spike (S) glycoprotein interacts with the human ACE2 receptor to mediate viral entry into host cells We report the cryo-EM structures of a tightly closed SARS-CoV-2 S trimer with packed fusion peptide and an ACE2-bound S trimer at 2 7- and 3 8-A resolution, respectively Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing motions Notably, the SARS-CoV-2 S trimer appears much more sensitive to the ACE2 receptor than the SARS-CoV S trimer regarding receptor-triggered transformation from the closed prefusion state to the fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2 We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2 Our findings depict the mechanism of ACE2-induced S trimer conformational transitions from the ground prefusion state toward the postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics
is ?:annotates of	<https://research.tib.eu/covid-19/entity/1b0hzcvs_hasAnnotation_C0020517> <https://research.tib.eu/covid-19/entity/1b0hzcvs_hasAnnotation_C1175743> <https://research.tib.eu/covid-19/entity/1b0hzcvs_hasAnnotation_C1422064> <https://research.tib.eu/covid-19/entity/1b0hzcvs_hasAnnotation_C5203676>
?:creator	<https://research.tib.eu/covid-19/entity/Xu%2C_C.%3B_Wang%2C_Y.%3B_Liu%2C_C.%3B_Zhang%2C_C.%3B_Han%2C_W.%3B_Hong%2C_X.%3B_Hong%2C_Q.%3B_Wang%2C_S.%3B_Zhao%2C_Q.%3B_Yang%2C_Y.%3B_Chen%2C_K.%3B_Zheng%2C_W.%3B_Kong%2C_L.%3B_Wang%2C_F.%3B_Zuo%2C_Q.%3B_Huang%2C_Z.%3B_Cong%2C_Y.> <https://research.tib.eu/covid-19/entity/Xu%2C_Cong%3B_Wang%2C_Yanxing%3B_Liu%2C_Caixuan%3B_Zhang%2C_Chao%3B_Han%2C_Wenyu%3B_Hong%2C_Xiaoyu%3B_Wang%2C_Yifan%3B_Hong%2C_Qin%3B_Wang%2C_Shutian%3B_Zhao%2C_Qiaoyu%3B_Wang%2C_Yalei%3B_Yang%2C_Yong%3B_Chen%2C_Kaijian%3B_Zheng%2C_Wei%3B_Kong%2C_Liangliang%3B_Wang%2C_Fangfang%3B_Zuo%2C_Qinyu%3B_Huang%2C_Zhong%3B_Cong%2C_Yao>
?:journal	Sci._Adv Science_Advances
?:license	unk
?:publication_isRelatedTo_Disease	<https://research.tib.eu/covid-19/entity/COVID-19>
is ?:relation_isRelatedTo_publication of	<https://research.tib.eu/covid-19/entity/1b0hzcvs_HAS_C0017968_INTERACTS_WITH_C1422064> <https://research.tib.eu/covid-19/entity/1b0hzcvs_HAS_C5203676_INTERACTS_WITH_C1175743>
?:source	WHO
?:title	Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM
?:type	<https://research.tib.eu/covid-19/vocab/Publication>
?:who_covidence_id	#1066790 #961000
?:year	2020 2021

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Value

?:abstract

The recent outbreaks and rapid international spread of SARS-CoV-2 pose a global health emergency. Its trimeric spike (S) glycoprotein interacts with human ACE2-receptor to mediate viral entry into host-cells. Here we present cryo-EM structures of a tightly closed SARS-CoV-2 S-trimer with packed fusion peptide, and an ACE2-bound S-trimer at 2.7 Å and 3.8 Å resolution, respectively. Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing-motions within the S-trimer. Noteworthy, SARS-CoV-2 S-trimer appears much more sensitive to ACE2-receptor than SARS-CoV S-trimer regarding receptor-triggered transformation from the closed prefusion state to fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2. We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2. Our findings depict the mechanism of ACE2-induced S-trimer conformational transitions from ground prefusion state toward postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics.
The recent outbreaks of SARS-CoV-2 pose a global health emergency The SARS-CoV-2 trimeric spike (S) glycoprotein interacts with the human ACE2 receptor to mediate viral entry into host cells We report the cryo-EM structures of a tightly closed SARS-CoV-2 S trimer with packed fusion peptide and an ACE2-bound S trimer at 2 7- and 3 8-A resolution, respectively Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing motions Notably, the SARS-CoV-2 S trimer appears much more sensitive to the ACE2 receptor than the SARS-CoV S trimer regarding receptor-triggered transformation from the closed prefusion state to the fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2 We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2 Our findings depict the mechanism of ACE2-induced S trimer conformational transitions from the ground prefusion state toward the postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics

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