scholarly journals Tuning the binding interface between Machupo virus glycoprotein and human transferrin receptor

2020 ◽  
Author(s):  
Dick J Sjöström ◽  
Anneli Lundgren ◽  
Scott J Garforth ◽  
Sinisa Bjelic
Keyword(s):  
Transferrin Receptor ◽  
Virus Glycoprotein ◽  
Human Transferrin ◽  
Binding Interface ◽  
Human Transferrin Receptor ◽  
Machupo Virus

scholarly journals Machupo Virus Glycoprotein Determinants for Human Transferrin Receptor 1 Binding and Cell Entry

PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e21398 ◽  
Author(s):  
Sheli R. Radoshitzky ◽  
Lindsay E. Longobardi ◽  
Jens H. Kuhn ◽  
Cary Retterer ◽  
Lian Dong ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Cell Entry ◽  
Virus Glycoprotein ◽  
Human Transferrin ◽  
Human Transferrin Receptor ◽  
Transferrin Receptor 1 ◽  
Machupo Virus

scholarly journals Investigation of Clade B New World Arenavirus Tropism by Using Chimeric GP1 Proteins

2009 ◽  
Vol 84 (2) ◽  
pp. 1176-1182 ◽  
Author(s):  
Vanessa K. Martin ◽  
Magali E. Droniou-Bonzom ◽  
Therese Reignier ◽  
Jill E. Oldenburg ◽  
Alex U. Cox ◽  
...  
Keyword(s):  
Central Region ◽  
Transferrin Receptor ◽  
New World ◽  
Receptor Type ◽  
Human Transferrin ◽  
Clade B ◽  
Human Transferrin Receptor ◽  
Machupo Virus ◽  
Different Characteristics

ABSTRACT 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.

scholarly journals Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Structure ◽  
1998 ◽  
Vol 6 (10) ◽  
pp. 1235-1243 ◽  
Author(s):  
Hendrik Fuchs ◽  
Uwe Lücken ◽  
Rudolf Tauber ◽  
Andreas Engel ◽  
Reinhard Geßner
Keyword(s):  
Electron Microscopy ◽  
Transferrin Receptor ◽  
Structural Model ◽  
Human Transferrin ◽  
Human Transferrin Receptor

The Promoter Region of the Human Transferrin Receptor Gene

1988 ◽  
Vol 526 (1 Hemochromatos) ◽  
pp. 54-64 ◽  
Author(s):  
John L. Casey ◽  
Bruno Jeso ◽  
Krishnamurthy Rao ◽  
Tracey A. Rouault ◽  
Richard D. Klausner ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Promoter Region ◽  
Receptor Gene ◽  
Human Transferrin ◽  
Human Transferrin Receptor

scholarly journals Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain.

1990 ◽  
Vol 1 (4) ◽  
pp. 369-377 ◽  
Author(s):  
T E McGraw ◽  
F R Maxfield
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rate Constant ◽  
Transferrin Receptor ◽  
Aromatic Amino Acid ◽  
Opposite Polarity ◽  
Receptor Internalization ◽  
Aromatic Side Chain ◽  
Human Transferrin ◽  
Human Transferrin Receptor

The objective of this work is to identify the elements of the human transferrin receptor that are involved in receptor internalization, intracellular sorting, and recycling. We have found that an aromatic side chain at position 20 on the cytoplasmic portion of the human transferrin receptor is required for efficient internalization. The wild-type human transferrin receptor has a tyrosine at this position. Replacement of the Tyr-20 with an aromatic amino acid does not alter the rate constant of internalization, whereas substitution with the nonaromatic amino acids serine, leucine, or cysteine reduces the internalization rate constant approximately three-fold. These results are consistent with similar studies of other receptor systems that have also documented the requirement for a tyrosine in rapid internalization. The amino terminus of the transferrin receptor is cytoplasmic, with the tyrosine 41 amino acids from the membrane. These two features distinguish the transferrin receptor from the other membrane proteins for which the role of tyrosine in internalization has been examined, because these proteins have the opposite polarity with respect to the membrane and because the tyrosines are located closer to the membrane (within 25 amino acids). The externalization rate for the recycling of the transferrin receptor is not altered by any of these substitutions, demonstrating that the aromatic amino acid internalization signal is not required for the efficient exocytosis of internalized receptor.

Identification of the O-linked glycosylation site of the human transferrin receptor

Glycobiology ◽  
1992 ◽  
Vol 2 (4) ◽  
pp. 355-359 ◽  
Author(s):  
Gary R. Hayes ◽  
Caroline A. Enns ◽  
John J. Lucas
Keyword(s):  
Transferrin Receptor ◽  
Glycosylation Site ◽  
Human Transferrin ◽  
Human Transferrin Receptor
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