Literature summary for 3.4.17.23 extracted from

Low-Gan, J.; Huang, R.; Kelley, A.; Jenkins, G.W.; McGregor, D.; Smider, V.V.
Diversity of ACE2 and its interaction with SARS-CoV-2 receptor binding domain (2021), Biochem. J., 478, 3671-3684 .

Search for more literature for 3.4.17.23

Cloned(Commentary)

Cloned (Comment)	Organism
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Homo sapiens
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Rhinolophus sinicus
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Felis catus
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Cricetulus griseus
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Mustela putorius
30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	XP_024843618.1	-	-
Cricetulus griseus	XP_003503283.12	-	-
Felis catus	Q56H28	-	-
Homo sapiens	Q9BYF1	-	-
Mustela putorius	Q2WG88	-	-
Rhinolophus sinicus	U5WHY8	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Homo sapiens
recombinant enzyme	Rhinolophus sinicus
recombinant enzyme	Felis catus
recombinant enzyme	Cricetulus griseus
recombinant enzyme	Mustela putorius
recombinant enzyme	Bos taurus

Synonyms

Synonyms	Comment	Organism
ACE2	-	Homo sapiens
ACE2	-	Rhinolophus sinicus
ACE2	-	Felis catus
ACE2	-	Cricetulus griseus
ACE2	-	Mustela putorius
ACE2	-	Bos taurus

General Information

General Information	Comment	Organism
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Homo sapiens
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Rhinolophus sinicus
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Felis catus
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Cricetulus griseus
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Mustela putorius
evolution	the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism	Bos taurus
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Homo sapiens
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Rhinolophus sinicus
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Felis catus
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Cricetulus griseus
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Mustela putorius
physiological function	SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection	Bos taurus

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Release 2023.1 (January 2023)