Tuning the binding interface between Machupo virus glycoprotein and human transferrin receptor. [PDF]
AbstractMachupo virus, known to cause hemorrhagic fevers, enters human cells via binding with its envelope glycoprotein to transferrin receptor 1 (TfR). Similarly, the receptor interactions have been explored in biotechnological applications as a molecular system to ferry therapeutics across the cellular membranes and through the impenetrable blood ...
Sjöström DJ +3 more
europepmc +8 more sources
RNA ligands activate the Machupo virus polymerase and guide promoter usage. [PDF]
Significance Atomic structures of the polymerase–endonuclease complex of the orthomyxovirus influenza and the orthobunyavirus La Crosse—two distinct segmented negative-sense (SNS) RNA viruses—demonstrate that binding of the genomic 5′ RNA rearranges the catalytic residues of the RNA-dependent RNA-polymerase (RdRP). Working with the arenavirus,
Pyle JD, Whelan SPJ.
europepmc +4 more sources
Characterization of a STAT-1 Knockout Mouse Model for Machupo Virus Infection and Pathogenesis [PDF]
Machupo virus (MACV), a member of the Arenaviridae family and causative agent of Bolivian hemorrhagic fever, results in lethality rates of 25–35% in humans.
Stephanie R. Monticelli +13 more
doaj +3 more sources
Monoclonal Antibodies with Neutralizing Activity and Fc-Effector Functions against the Machupo Virus Glycoprotein. [PDF]
MACV infections are a significant public health concern and lead to high case fatality rates. No specific treatment or vaccine for MACV infections exist. However, cases of Junin virus infection, a related virus, can be treated with convalescent-phase serum. This indicates that a MAb-based therapy for MACV could be effective.
Amanat F +5 more
europepmc +5 more sources
Development and characterization of a reverse genetics system for the lineage II Chicava strain of Machupo virus in a guinea pig model. [PDF]
BackgroundMachupo virus (MACV) is a New World mammarenavirus (hereafter referred to as "arenavirus") and the etiologic agent of Bolivian hemorrhagic fever (BHF).
Emily Mantlo +5 more
doaj +3 more sources
Isothermal real-time RT-RPA for Machupo virus detection: Field-adaptable sensitivity comparable with laboratory PCR. [PDF]
Isothermal nucleic acid amplification methods, such as recombinase polymerase amplification (RPA), are becoming increasingly vital as diagnostic platforms for neglected tropical diseases by enabling rapid and accurate detection in under-resourced regions.
Marina A Kapitonova +5 more
doaj +3 more sources
Assembly of a functional Machupo virus polymerase complex. [PDF]
Segmented negative-sense viruses of the family Arenaviridae encode a large polymerase (L) protein that contains all of the enzymatic activities required for RNA synthesis. These activities include an RNA-dependent RNA polymerase (RdRP) and an RNA endonuclease that cleaves capped primers from ...
Kranzusch PJ +6 more
europepmc +6 more sources
Unusual molecular architecture of the machupo virus attachment glycoprotein. [PDF]
ABSTRACTNew World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor.
Bowden TA +6 more
europepmc +6 more sources
The Ectodomain of Glycoprotein from the Candid#1 Vaccine Strain of Junin Virus Rendered Machupo Virus Partially Attenuated in Mice Lacking IFN-αβ/γ Receptor. [PDF]
Machupo virus (MACV), a New World arenavirus, is the etiological agent of Bolivian hemorrhagic fever (BHF). Junin virus (JUNV), a close relative, causes Argentine hemorrhagic fever (AHF).
Takaaki Koma +7 more
doaj +3 more sources
Machupo Virus Expressing GPC of the Candid#1 Vaccine Strain of Junin Virus Is Highly Attenuated and Immunogenic. [PDF]
ABSTRACT Machupo virus (MACV) is the causative agent of Bolivian hemorrhagic fever. Our previous study demonstrated that a MACV strain with a single amino acid substitution (F438I) in the transmembrane domain of glycoprotein is attenuated but genetically unstable in mice.
Koma T +9 more
europepmc +5 more sources

