Investigation of clade B New World arenavirus tropism by using chimeric GP1 proteins.
Clade B of the New World arenaviruses contains both pathogenic and nonpathogenic members, whose surface glycoproteins (GPs) are characterized by different abilities to use the human transferrin receptor type 1 (hTfR1) protein as a receptor. Using closely related pairs of pathogenic and nonpathogenic viruses, we investigated the determinants of the GP1 subunit that confer these different characteristics. We identified a central region (residues 85 to 221) in the Guanarito virus GP1 that was sufficient to interact with hTfR1, with residues 159 to 221 being essential. The recently solved structure of part of the Machupo virus GP1 suggests an explanation for these requirements.
Martin
Vanessa K
VK
USC Keck School of Medicine, 2011 Zonal Avenue, HMR502, Los Angeles, CA 90033, USA.
Droniou-Bonzom
Magali E
ME
Reignier
Therese
T
Oldenburg
Jill E
JE
Cox
Alex U
AU
Cannon
Paula M
PM
D000595:Amino Acid Sequence; D000818:Animals; D006477:Arenaviruses, New World / Q000145:classification / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology*; D016466:CHO Cells; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011990:Receptors, Transferrin / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D006023:Glycoproteins; D011990:Receptors, Transferrin; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins