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Article ; Online: Monoclonal antibody therapy demonstrates increased virulence of a lineage VII strain of Lassa virus in nonhuman primates.

Woolsey, Courtney / Cross, Robert W / Prasad, Abhishek N / Agans, Krystle N / Borisevich, Viktoriya / Deer, Daniel J / Dobias, Natalie S / Fears, Alyssa C / Harrison, Mack B / Heinrich, Megan L / Fenton, Karla A / Garry, Robert F / Branco, Luis M / Geisbert, Thomas W

Emerging microbes & infections

2024 Volume 13, Issue 1, Page(s) 2301061

Abstract: Lassa virus (LASV) is a World Health Organization (WHO) priority pathogen that causes high morbidity and mortality. Recently, we showed that a combination of three broadly neutralizing human monoclonal antibodies known as Arevirumab-3 (8.9F, 12.1F, 37.2D) ...

Abstract	Lassa virus (LASV) is a World Health Organization (WHO) priority pathogen that causes high morbidity and mortality. Recently, we showed that a combination of three broadly neutralizing human monoclonal antibodies known as Arevirumab-3 (8.9F, 12.1F, 37.2D) based on the lineage IV Josiah strain protected 100% of cynomolgus macaques against heterologous challenge with lineage II and III strains of LASV when therapy was initiated beginning at day 8 after challenge. LASV strains from Benin and Togo represent a new lineage VII that are more genetically diverse from lineage IV than strains from lineages II and III. Here, we tested the ability of Arevirumab-3 to protect macaques against a LASV lineage VII Togo isolate when treatment was administered beginning 8 days after exposure. Unexpectedly, only 40% of treated animals survived challenge. In a subsequent study we showed that Arevirumab-3 protected 100% of macaques from lethal challenge when treatment was initiated 7 days after LASV Togo exposure. Based on our transcriptomics data, successful Arevirumab-3 treatment correlated with diminished neutrophil signatures and the predicted development of T cell responses. As the
MeSH term(s)	Humans ; Animals ; Lassa virus ; Lassa Fever ; Virulence ; Macaca fascicularis ; Antibodies, Monoclonal/pharmacology
Chemical Substances	Antibodies, Monoclonal
Language	English
Publishing date	2024-01-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	2681359-2
ISSN	2222-1751 ; 2222-1751
ISSN (online)	2222-1751
ISSN	2222-1751
DOI	10.1080/22221751.2023.2301061
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Article ; Online: Monoclonal antibody therapy protects nonhuman primates against mucosal exposure to Lassa virus.

Cross, Robert W / Fenton, Karla A / Woolsey, Courtney / Prasad, Abhishek N / Borisevich, Viktoriya / Agans, Krystle N / Deer, Daniel J / Dobias, Natalie S / Fears, Alyssa C / Heinrich, Megan L / Geisbert, Joan B / Garry, Robert F / Branco, Luis M / Geisbert, Thomas W

Cell reports. Medicine

2024 Volume 5, Issue 2, Page(s) 101392

Abstract: Lassa fever (LF) is an acute viral illness that causes thousands of deaths annually in West Africa. There are currently no Lassa virus (LASV) vaccines or antivirals approved for human use. Recently, we showed that combinations of broadly neutralizing ... ...

Abstract	Lassa fever (LF) is an acute viral illness that causes thousands of deaths annually in West Africa. There are currently no Lassa virus (LASV) vaccines or antivirals approved for human use. Recently, we showed that combinations of broadly neutralizing human monoclonal antibodies (BNhuMAbs) known as Arevirumab-2 or Arevirumab-3 protected up to 100% of cynomolgus macaques against challenge with diverse lineages of LASV when treatment was initiated at advanced stages of disease. This previous work assessed efficacy against parenteral exposure. However, transmission of LASV to humans occurs primarily by mucosal exposure to virus shed from Mastomys rodents. Here, we describe the development of a lethal intranasal exposure macaque model of LF. This model is employed to show that Arevirumab cocktails rescue 100% of macaques from lethal LASV infection when treatment is initiated 8 days after LASV exposure. Our work demonstrates BNhuMAbs have utility in treating LASV infection acquired through mucosal exposure.
MeSH term(s)	Animals ; Humans ; Lassa virus ; Lassa Fever/drug therapy ; Lassa Fever/prevention & control ; Macaca fascicularis ; Immunotherapy ; Antibodies, Monoclonal/pharmacology ; Antibodies, Monoclonal/therapeutic use
Chemical Substances	Antibodies, Monoclonal
Language	English
Publishing date	2024-01-26
Publishing country	United States
Document type	Journal Article
ISSN	2666-3791
ISSN (online)	2666-3791
DOI	10.1016/j.xcrm.2024.101392
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Article ; Online: Elevated L-threonine is a biomarker for Lassa fever and Ebola.

Gale, Trevor V / Schieffelin, John S / Branco, Luis M / Garry, Robert F / Grant, Donald S

Virology journal

2020 Volume 17, Issue 1, Page(s) 188

Abstract: Background: Lassa fever and Ebola are characterized by non-specific initial presentations that can progress to severe multisystem illnesses with high fatality rates. Samples from additional subjects are examined to extend and corroborate biomarkers with ...

Abstract	Background: Lassa fever and Ebola are characterized by non-specific initial presentations that can progress to severe multisystem illnesses with high fatality rates. Samples from additional subjects are examined to extend and corroborate biomarkers with prognostic value for these diseases. Methods: Liquid Chromatography Mass Spectrometry metabolomics was used to identify and confirm metabolites disrupted in the blood of Lassa fever and Ebola patients. Authenticated standards are used to confirm the identify of key metabolites. Results: We confirm prior results by other investigators that the amino acid L-threonine is elevated during Ebola virus infection. L-Threonine is also elevated during Lassa virus infection. We also confirmed that platelet-activating factor (PAF) and molecules with PAF moiety are reduced in the blood of patients with fatal Lassa fever. Similar changes in PAF and PAF-like molecules were not observed in the blood of Ebola patients. Conclusions: Metabolomics may provide tools to identify pathways that are differentially affected during viral hemorrhagic fevers and guide development of diagnostics to monitor and predict outcome.
MeSH term(s)	Adolescent ; Adult ; Biomarkers/blood ; Child ; Child, Preschool ; Chromatography, Liquid/methods ; Cohort Studies ; Female ; Hemorrhagic Fever, Ebola/blood ; Hemorrhagic Fever, Ebola/diagnosis ; Hemorrhagic Fever, Ebola/metabolism ; Humans ; Infant ; Lassa Fever/blood ; Lassa Fever/diagnosis ; Lassa Fever/metabolism ; Male ; Mass Spectrometry/methods ; Metabolomics ; Middle Aged ; Threonine/blood ; Threonine/genetics ; Young Adult
Chemical Substances	Biomarkers ; Threonine (2ZD004190S)
Language	English
Publishing date	2020-11-26
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1743-422X
ISSN (online)	1743-422X
DOI	10.1186/s12985-020-01459-y
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Article ; Online: A human monoclonal antibody combination rescues nonhuman primates from advanced disease caused by the major lineages of Lassa virus.

Cross, Robert W / Heinrich, Megan L / Fenton, Karla A / Borisevich, Viktoriya / Agans, Krystle N / Prasad, Abhishek N / Woolsey, Courtney / Deer, Daniel J / Dobias, Natalie S / Rowland, Megan M / Lathigra, Raju / Borrega, Rodrigo / Geisbert, Joan B / Garry, Robert F / Branco, Luis M / Geisbert, Thomas W

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 34, Page(s) e2304876120

Abstract: There are no approved treatments for Lassa fever (LF), which is responsible for thousands of deaths each year in West Africa. A major challenge in developing effective medical countermeasures against LF is the high diversity of circulating Lassa virus ( ... ...

Abstract	There are no approved treatments for Lassa fever (LF), which is responsible for thousands of deaths each year in West Africa. A major challenge in developing effective medical countermeasures against LF is the high diversity of circulating Lassa virus (LASV) strains with four recognized lineages and four proposed lineages. The recent resurgence of LASV in Nigeria caused by genetically distinct strains underscores this concern. Two LASV lineages (II and III) are dominant in Nigeria. Here, we show that combinations of two or three pan-lineage neutralizing human monoclonal antibodies (8.9F, 12.1F, 37.D) known as Arevirumab-2 or Arevirumab-3 can protect up to 100% of cynomolgus macaques against challenge with both lineage II and III LASV isolates when treatment is initiated at advanced stages of disease on day 8 after LASV exposure. This work demonstrates that it may be possible to develop postexposure interventions that can broadly protect against most strains of LASV.
MeSH term(s)	Animals ; Humans ; Lassa virus ; Lassa Fever/prevention & control ; Africa, Western ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; Macaca fascicularis
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing
Language	English
Publishing date	2023-08-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2304876120
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Article ; Online: Delineating the mechanism of anti-Lassa virus GPC-A neutralizing antibodies.

Enriquez, Adrian S / Buck, Tierra K / Li, Haoyang / Norris, Michael J / Moon-Walker, Alex / Zandonatti, Michelle A / Harkins, Stephanie S / Robinson, James E / Branco, Luis M / Garry, Robert F / Saphire, Erica Ollmann / Hastie, Kathryn M

Cell reports

2022 Volume 39, Issue 8, Page(s) 110841

Abstract: Lassa virus (LASV) is the etiologic agent of Lassa Fever, a hemorrhagic disease that is endemic to West Africa. During LASV infection, LASV glycoprotein (GP) engages with multiple host receptors for cell entry. Neutralizing antibodies against GP are rare ...

Abstract	Lassa virus (LASV) is the etiologic agent of Lassa Fever, a hemorrhagic disease that is endemic to West Africa. During LASV infection, LASV glycoprotein (GP) engages with multiple host receptors for cell entry. Neutralizing antibodies against GP are rare and principally target quaternary epitopes displayed only on the metastable, pre-fusion conformation of GP. Currently, the structural features of the neutralizing GPC-A antibody competition group are understudied. Structures of two GPC-A antibodies presented here demonstrate that they bind the side of the pre-fusion GP trimer, bridging the GP1 and GP2 subunits. Complementary biochemical analyses indicate that antibody 25.10C, which is broadly specific, neutralizes by inhibiting binding of the endosomal receptor LAMP1 and also by blocking membrane fusion. The other GPC-A antibody, 36.1F, which is lineage-specific, prevents LAMP1 association only. These data illuminate a site of vulnerability on LASV GP and will guide efforts to elicit broadly reactive therapeutics and vaccines.
MeSH term(s)	Antibodies, Neutralizing ; Epitopes ; Glycoproteins/metabolism ; Humans ; Lassa Fever/prevention & control ; Lassa virus/metabolism ; Viral Envelope Proteins
Chemical Substances	Antibodies, Neutralizing ; Epitopes ; Glycoproteins ; Viral Envelope Proteins
Language	English
Publishing date	2022-05-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110841
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Article ; Online: Evaluating the A-Subunit of the Heat-Labile Toxin (LT) As an Immunogen and a Protective Antigen Against Enterotoxigenic Escherichia coli (ETEC).

Norton, Elizabeth B / Branco, Luis M / Clements, John D

PloS one

2015 Volume 10, Issue 8, Page(s) e0136302

Abstract: Diarrheal illness contributes to malnutrition, stunted growth, impaired cognitive development, and high morbidity rates in children worldwide. Enterotoxigenic Escherichia coli (ETEC) is a major contributor to this diarrheal disease burden. ETEC cause ... ...

Abstract	Diarrheal illness contributes to malnutrition, stunted growth, impaired cognitive development, and high morbidity rates in children worldwide. Enterotoxigenic Escherichia coli (ETEC) is a major contributor to this diarrheal disease burden. ETEC cause disease in the small intestine by means of colonization factors and by production of a heat-labile enterotoxin (LT) and/or a small non-immunogenic heat-stable enterotoxin (ST). Overall, the majority of ETEC produce both ST and LT. LT induces secretion via an enzymatically active A-subunit (LT-A) and a pentameric, cell-binding B-subunit (LT-B). The importance of anti-LT antibodies has been demonstrated in multiple clinical and epidemiological studies, and a number of potential ETEC vaccine candidates have included LT-B as an important immunogen. However, there is limited information about the potential contribution of LT-A to development of protective immunity. In the current study, we evaluate the immune response against the A-subunit of LT as well as the A-subunit's potential as a protective antigen when administered alone or in combination with the B-subunit of LT. We evaluated human sera from individuals challenged with a prototypic wild-type ETEC strain as well as sera from individuals living in an ETEC endemic area for the presence of anti-LT, anti-LT-A and anti-LT-B antibodies. In both cases, a significant number of individuals intentionally or endemically infected with ETEC developed antibodies against both LT subunits. In addition, animals immunized with the recombinant proteins developed robust antibody responses that were able to neutralize the enterotoxic and cytotoxic effects of native LT by blocking binding and entry into cells (anti-LT-B) or the intracellular enzymatic activity of the toxin (anti-LT-A). Moreover, antibodies to both LT subunits acted synergistically to neutralize the holotoxin when combined. Taken together, these data support the inclusion of both LT-A and LT-B in prospective vaccines against ETEC.
MeSH term(s)	Animals ; Antibodies, Bacterial/blood ; Antibodies, Bacterial/immunology ; Antibodies, Neutralizing/blood ; Antibodies, Neutralizing/immunology ; Antigens, Bacterial/genetics ; Antigens, Bacterial/immunology ; Bacterial Toxins/chemistry ; Bacterial Toxins/genetics ; Bacterial Toxins/immunology ; Cell Line ; Disease Models, Animal ; Enterotoxigenic Escherichia coli/genetics ; Enterotoxigenic Escherichia coli/immunology ; Enterotoxins/chemistry ; Enterotoxins/genetics ; Enterotoxins/immunology ; Escherichia coli Infections/epidemiology ; Escherichia coli Infections/immunology ; Escherichia coli Infections/prevention & control ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/immunology ; Humans ; Immunity, Mucosal ; Immunization ; Mice ; Mucous Membrane/immunology ; Mucous Membrane/microbiology ; Neutralization Tests ; Protein Subunits/genetics ; Protein Subunits/immunology
Chemical Substances	Antibodies, Bacterial ; Antibodies, Neutralizing ; Antigens, Bacterial ; Bacterial Toxins ; Enterotoxins ; Escherichia coli Proteins ; Protein Subunits ; heat-labile enterotoxin, E coli (D9K3SN2LNY)
Language	English
Publishing date	2015-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0136302
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Article ; Online: Neutralizing Antibodies against Lassa Virus Lineage I.

Buck, Tierra K / Enriquez, Adrian S / Schendel, Sharon L / Zandonatti, Michelle A / Harkins, Stephanie S / Li, Haoyang / Moon-Walker, Alex / Robinson, James E / Branco, Luis M / Garry, Robert F / Saphire, Erica Ollmann / Hastie, Kathryn M

mBio

2022 Volume 13, Issue 4, Page(s) e0127822

Abstract: Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage ...

Abstract	Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage I LASV evades neutralization by half of known antibodies in the GPC-A antibody competition group and all but one of the antibodies in the GPC-B competition group. Here, we solve two cryo-electron microscopy (cryo-EM) structures of LI GP in complex with a GPC-A and a GPC-B antibody. We used complementary structural and biochemical techniques to identify single-amino-acid substitutions in LI that are responsible for immune evasion by each antibody group. Further, we show that LI infection is more dependent on the endosomal receptor lysosome-associated membrane protein 1 (LAMP1) for viral entry relative to LIV. In the absence of LAMP1, LI requires a more acidic fusion pH to initiate membrane fusion with the host cell relative to LIV.
MeSH term(s)	Antibodies, Neutralizing ; Cryoelectron Microscopy ; Humans ; Lassa Fever ; Lassa virus/genetics ; Virus Internalization
Chemical Substances	Antibodies, Neutralizing
Language	English
Publishing date	2022-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.01278-22
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Article ; Online: Host Proteins Identified in Extracellular Viral Particles as Targets for Broad-Spectrum Antiviral Inhibitors.

Gale, Trevor V / Horton, Timothy M / Hoffmann, Andrew R / Branco, Luis M / Garry, Robert F

Journal of proteome research

2018 Volume 18, Issue 1, Page(s) 7–17

Abstract: Liquid chromatography mass spectrometry (LCMS) proteomic analyses have revealed that host proteins are often captured in extracellular virions. These proteins may play a role in viral replication or infectivity and can represent targets for broad- ... ...

Abstract	Liquid chromatography mass spectrometry (LCMS) proteomic analyses have revealed that host proteins are often captured in extracellular virions. These proteins may play a role in viral replication or infectivity and can represent targets for broad-spectrum antiviral agent development. We utilized LCMS to determine the host protein composition of Lassa virus-like particles (LASV VLPs). Multiple host proteins incorporated in LASV VLPs are also incorporated in unrelated viruses, notably ribosomal proteins. We assembled a data set of host proteins incorporated into extracellular viral particles. The frequent incorporation of specific host proteins into viruses of diverse families suggests that interactions of these proteins with viral factors may be important for effective viral replication. Drugs that target virion-associated host proteins could affect the protein in the extracellular virion or the host cell. Compounds that target proteins incorporated into virions with high frequency, but with no known antiviral activity, were assayed in a scalable viral screening platform, and hits were tested in competent viral systems. One of these molecules, GAPDH modulating small molecule CGP 3466B maleate (Omigapil), exhibited a dose-dependent inhibition of HIV, dengue virus, and Zika virus.
MeSH term(s)	Antiviral Agents/pharmacology ; Chromatography, Liquid ; Dengue Virus/drug effects ; Drug Discovery/methods ; HIV/drug effects ; Host-Pathogen Interactions ; Mass Spectrometry ; Oxepins/pharmacology ; Proteomics/methods ; Virion/chemistry ; Zika Virus/drug effects
Chemical Substances	Antiviral Agents ; Oxepins ; dibenzo(b,f)oxepin-10-ylmethyl-methyl-prop-2-ynyl-amine
Language	English
Publishing date	2018-11-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.8b00204
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Article ; Online: Characterization of the Lassa virus GP1 ectodomain shedding: implications for improved diagnostic platforms.

Branco, Luis M / Garry, Robert F

Virology journal

2009 Volume 6, Page(s) 147

Abstract: Background: There is a significant requirement for the development and acquisition of reagents that will facilitate effective diagnosis, treatment, and prevention of Lassa fever. In this regard, detection of early markers of Lassa virus (LASV) infection ...

Abstract	Background: There is a significant requirement for the development and acquisition of reagents that will facilitate effective diagnosis, treatment, and prevention of Lassa fever. In this regard, detection of early markers of Lassa virus (LASV) infection may improve diagnosis and ultimately successful treatment with antivirals. Characterization of LASV GP1 ectodomain shedding is an important step toward developing sensitive diagnostics to detect circulating levels of this viral glycoprotein in infected patient sera. Results: Secretion of GP1 from mammalian cells expressing a native LASV GPC gene was not mediated by proteolytic cleavage, as determined by treatment with a panel of matrix metalloprotease (MMP) inhibitors. The shedding of GP1 was also not the result of over-expression of GPC under the control of a strong intron-A containing CMV promoter, as the soluble component could be immunoprecipitated from supernatants of cells expressing low levels of GPC under the control of an intronless promoter. Cells transfected with GPC retained surface membrane-associated expression of GP1 as determined by immunofluorescence assay, in addition to secreting the glycoprotein.Secreted GP1 derived from GPC expression has a higher content of high mannose N-linked glycosylation than sGP1 expressed independently from the GP2 portion of the protein. Neither GP1 isoform contains sialylated N-glycans, O-linked carbohydrate chains, or galactose-beta(1-4)-N-acetylglucosamine commonly present in complex and hybrid N-glycan structures. Conclusion: These results demonstrate the non-proteolytic secretory nature of GP1 shedding during expression of the arenaviral glycoprotein complex. This phenomenon parallels shedding of a secretory glycoprotein component in filovirus replication. The glycosylation pattern of soluble GP1 resulting from expression of GPC was different from that of a soluble GP1 construct (sGP1-RRAA-FLAG), highlighting the intricately orchestrated post translational processing of the LASV glycoprotein complex.
MeSH term(s)	Cell Line ; Glycosylation ; Humans ; Lassa virus/physiology ; Models, Biological ; Protein Processing, Post-Translational ; Viral Envelope Proteins/metabolism ; Virus Replication
Chemical Substances	Viral Envelope Proteins ; glycoprotein gp1, lassa virus
Language	English
Publishing date	2009-09-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2160640-7
ISSN	1743-422X ; 1743-422X
ISSN (online)	1743-422X
ISSN	1743-422X
DOI	10.1186/1743-422X-6-147
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Article ; Online: Characterization of the Lassa virus GP1 ectodomain shedding

Branco Luis M / Garry Robert F

Virology Journal, Vol 6, Iss 1, p

implications for improved diagnostic platforms

2009 Volume 147

Abstract: Abstract Background There is a significant requirement for the development and acquisition of reagents that will facilitate effective diagnosis, treatment, and prevention of Lassa fever. In this regard, detection of early markers of Lassa virus (LASV) ... ...

Abstract	Abstract Background There is a significant requirement for the development and acquisition of reagents that will facilitate effective diagnosis, treatment, and prevention of Lassa fever. In this regard, detection of early markers of Lassa virus (LASV) infection may improve diagnosis and ultimately successful treatment with antivirals. Characterization of LASV GP1 ectodomain shedding is an important step toward developing sensitive diagnostics to detect circulating levels of this viral glycoprotein in infected patient sera. Results Secretion of GP1 from mammalian cells expressing a native LASV GPC gene was not mediated by proteolytic cleavage, as determined by treatment with a panel of matrix metalloprotease (MMP) inhibitors. The shedding of GP1 was also not the result of over-expression of GPC under the control of a strong intron-A containing CMV promoter, as the soluble component could be immunoprecipitated from supernatants of cells expressing low levels of GPC under the control of an intronless promoter. Cells transfected with GPC retained surface membrane-associated expression of GP1 as determined by immunofluorescence assay, in addition to secreting the glycoprotein. Secreted GP1 derived from GPC expression has a higher content of high mannose N-linked glycosylation than sGP1 expressed independently from the GP2 portion of the protein. Neither GP1 isoform contains sialylated N-glycans, O-linked carbohydrate chains, or galactose-β(1-4)-N-acetylglucosamine commonly present in complex and hybrid N-glycan structures. Conclusion These results demonstrate the non-proteolytic secretory nature of GP1 shedding during expression of the arenaviral glycoprotein complex. This phenomenon parallels shedding of a secretory glycoprotein component in filovirus replication. The glycosylation pattern of soluble GP1 resulting from expression of GPC was different from that of a soluble GP1 construct (sGP1-RRAA-FLAG), highlighting the intricately orchestrated post translational processing of the LASV glycoprotein complex.
Keywords	Microbiology ; QR1-502 ; Science ; Q ; DOAJ:Microbiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences ; Medicine (General) ; R5-920 ; Medicine ; R ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Subject code	570
Language	English
Publishing date	2009-09-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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