scholarly journals Diversity of the 47-kD HtrA Nucleic Acid and Translated Amino Acid Sequences from 17 Recent Human Isolates ofOrientia

2013 ◽  
Vol 13 (6) ◽  
pp. 367-375 ◽  
Author(s):  
Ju Jiang ◽  
Daniel H. Paris ◽  
Stuart D. Blacksell ◽  
Nuntipa Aukkanit ◽  
Paul N. Newton ◽  
...  
1985 ◽  
Vol 13 (5) ◽  
pp. 1493-1504 ◽  
Author(s):  
Salomé Prat ◽  
Jordi Cortadas ◽  
Pere Puigdomènech ◽  
Jaume Palau

2021 ◽  
Vol 9 (8) ◽  
pp. 1606
Author(s):  
Oluwatoyin Areo ◽  
Pratik U. Joshi ◽  
Mark Obrenovich ◽  
Moncef Tayahi ◽  
Caryn L. Heldt

SARS-CoV-2, the cause of COVID-19, is a new, highly pathogenic coronavirus, which is the third coronavirus to emerge in the past 2 decades and the first to become a global pandemic. The virus has demonstrated itself to be extremely transmissible and deadly. Recent data suggest that a targeted approach is key to mitigating infectivity. Due to the proliferation of cataloged protein and nucleic acid sequences in databases, the function of the nucleic acid, and genetic encoded proteins, we make predictions by simply aligning sequences and exploring their homology. Thus, similar amino acid sequences in a protein usually confer similar biochemical function, even from distal or unrelated organisms. To understand viral transmission and adhesion, it is key to elucidate the structural, surface, and functional properties of each viral protein. This is typically first modeled in highly pathogenic species by exploring folding, hydrophobicity, and isoelectric point (IEP). Recent evidence from viral RNA sequence modeling and protein crystals have been inadequate, which prevent full understanding of the IEP and other viral properties of SARS-CoV-2. We have thus experimentally determined the IEP of SARS-CoV-2. Our findings suggest that for enveloped viruses, such as SARS-CoV-2, estimates of IEP by the amino acid sequence alone may be unreliable. We compared the experimental IEP of SARS-CoV-2 to variants of interest (VOIs) using their amino acid sequence, thus providing a qualitative comparison of the IEP of VOIs.


2003 ◽  
Vol 77 (7) ◽  
pp. 3950-3961 ◽  
Author(s):  
Angela M. I. Lam ◽  
David Keeney ◽  
Patrick Q. Eckert ◽  
David N. Frick

ABSTRACT The NS3 ATPase/helicase was isolated and characterized from three different infectious clones of hepatitis C virus (HCV). One helicase was from a genotype that normally responds to therapy (Hel-2a), and the other two were from more resistant genotypes, 1a (Hel-1a) and 1b (Hel-1b). Although the differences among these helicases are generally minor, all three enzymes have distinct properties. Hel-1a is less selective for nucleoside triphosphates, Hel-1b hydrolyzes nucleoside triphosphates less rapidly, and Hel-2a unwinds DNA more rapidly and binds DNA more tightly than the other two enzymes. Unlike related proteins, different nucleic acid sequences stimulate ATP hydrolysis by HCV helicase at different maximum rates and with different apparent efficiencies. This nucleic acid stimulation profile is conserved among the enzymes, but it does not result entirely from differential DNA-binding affinities. Although the amino acid sequences of the three proteins differ by up to 15%, one variant amino acid that is critical for helicase action was identified. NS3 residue 450 is a threonine in Hel-1a and Hel-1b and is an isoleucine in Hel-2a. A mutant Hel-1a with an isoleucine substituted for threonine 450 unwinds DNA more rapidly and binds DNA more tightly than the parent protein.


1997 ◽  
Author(s):  
G. Myers ◽  
B. Foley ◽  
B. Korber ◽  
J.W. Mellors ◽  
K.T. Jeang ◽  
...  

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