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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: A cocktail of protective antibodies subverts the dense glycan shield of Lassa virus.

Li, Haoyang / Buck, Tierra / Zandonatti, Michelle / Yin, Jieyun / Moon-Walker, Alex / Fang, Jingru / Koval, Anatoliy / Heinrich, Megan L / Rowland, Megan M / Diaz Avalos, Ruben / Schendel, Sharon L / Parekh, Diptiben / Zyla, Dawid / Enriquez, Adrian / Harkins, Stephanie / Sullivan, Brian / Smith, Victoria / Chukwudozie, Onyeka / Watanabe, Reika /

Robinson, James E / Garry, Robert F / Branco, Luis M / Hastie, Kathryn M / Saphire, Erica Ollmann

Science translational medicine

2022 Volume 14, Issue 668, Page(s) eabq0991

Abstract: Developing potent therapeutics and effective vaccines are the ultimate goals in controlling infectious diseases. Lassa virus (LASV), the causative pathogen of Lassa fever (LF), infects hundreds of thousands annually, but effective antivirals or vaccines ... ...

Abstract	Developing potent therapeutics and effective vaccines are the ultimate goals in controlling infectious diseases. Lassa virus (LASV), the causative pathogen of Lassa fever (LF), infects hundreds of thousands annually, but effective antivirals or vaccines against LASV infection are still lacking. Furthermore, neutralizing antibodies against LASV are rare. Here, we describe biochemical analyses and high-resolution cryo-electron microscopy structures of a therapeutic cocktail of three broadly protective antibodies that target the LASV glycoprotein complex (GPC), previously identified from survivors of multiple LASV infections. Structural and mechanistic analyses reveal compatible neutralizing epitopes and complementary neutralization mechanisms that offer high potency, broad range, and resistance to escape. These antibodies either circumvent or exploit specific glycans comprising the extensive glycan shield of GPC. Further, they require mammalian glycosylation, native GPC cleavage, and proper GPC trimerization. These findings guided engineering of a next-generation GPC antigen suitable for future neutralizing antibody and vaccine discovery. Together, these results explain protective mechanisms of rare, broad, and potent antibodies and identify a strategy for the rational design of therapeutic modalities against LF and related infectious diseases.
MeSH term(s)	Animals ; Humans ; Lassa virus ; Cryoelectron Microscopy ; Viral Vaccines ; Lassa Fever ; Antibodies, Neutralizing ; Epitopes ; Glycoproteins ; Polysaccharides ; Antiviral Agents ; Mammals
Chemical Substances	Viral Vaccines ; Antibodies, Neutralizing ; Epitopes ; Glycoproteins ; Polysaccharides ; Antiviral Agents
Language	English
Publishing date	2022-10-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2518854-9
ISSN	1946-6242 ; 1946-6234
ISSN (online)	1946-6242
ISSN	1946-6234
DOI	10.1126/scitranslmed.abq0991
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Article: Space-Time Trends in Lassa Fever in Sierra Leone by ELISA Serostatus, 2012–2019

Microorganisms. 2021 Mar. 12, v. 9, no. 3

2021

Abstract: Lassa fever (LF) is a viral hemorrhagic disease found in Sub-Saharan Africa and is responsible for up to 300,000 cases and 5000 deaths annually. LF is highly endemic in Sierra Leone, particularly in its Eastern Province. Kenema Government Hospital (KGH) ... ...

Abstract	Lassa fever (LF) is a viral hemorrhagic disease found in Sub-Saharan Africa and is responsible for up to 300,000 cases and 5000 deaths annually. LF is highly endemic in Sierra Leone, particularly in its Eastern Province. Kenema Government Hospital (KGH) maintains one of only a few LF isolation facilities in the world with year-round diagnostic testing. Here we focus on space-time trends for LF occurring in Sierra Leone between 2012 and 2019 to provide a current account of LF in the wake of the 2014–2016 Ebola epidemic. Data were analyzed for 3277 suspected LF cases and classified as acute, recent, and non-LF or prior LF exposure using enzyme-linked immunosorbent assays (ELISAs). Presentation rates for acute, recent, and non-LF or prior LF exposure were 6.0% (195/3277), 25.6% (838/3277), and 68.4% (2244/3277), respectively. Among 2051 non-LF or prior LF exposures, 33.2% (682/2051) tested positive for convalescent LF exposure. The overall LF case-fatality rate (CFR) was 78.5% (106/135). Both clinical presentations and confirmed LF cases declined following the Ebola epidemic. These declines coincided with an increased duration between illness onset and clinical presentation, perhaps suggesting more severe disease or presentation at later stages of illness. Acute LF cases and their corresponding CFRs peaked during the dry season (November to April). Subjects with recent (but not acute) LF exposure were more likely to present during the rainy season (May to October) than the dry season (p < 0.001). The findings here suggest that LF remains endemic in Sierra Leone and that caseloads are likely to resume at levels observed prior to the Ebola epidemic. The results provide insight on the current epidemiological profile of LF in Sierra Leone to facilitate LF vaccine studies and accentuate the need for LF cohort studies and continued advancements in LF diagnostics.
Keywords	Lassa virus fever ; diagnostic techniques ; disease severity ; dry season ; hospitals ; mortality ; space and time ; vaccines ; wet season ; Sierra Leone
Language	English
Dates of publication	2021-0312
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms9030586
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Article: Convergent Structures Illuminate Features for Germline Antibody Binding and Pan-Lassa Virus Neutralization

Hastie, Kathryn M / Cross, Robert W / Harkins, Stephanie S / Zandonatti, Michelle A / Koval, Anatoliy P / Heinrich, Megan L / Rowland, Megan M / Robinson, James E / Geisbert, Thomas W / Garry, Robert F / Branco, Luis M / Saphire, Erica Ollmann

Cell. 2019 Aug. 08, v. 178, no. 4

2019

Abstract: Lassa virus (LASV) causes hemorrhagic fever and is endemic in West Africa. Protective antibody responses primarily target the LASV surface glycoprotein (GPC), and GPC-B competition group antibodies often show potent neutralizing activity in humans. ... ...

Abstract	Lassa virus (LASV) causes hemorrhagic fever and is endemic in West Africa. Protective antibody responses primarily target the LASV surface glycoprotein (GPC), and GPC-B competition group antibodies often show potent neutralizing activity in humans. However, which features confer potent and broadly neutralizing antibody responses is unclear. Here, we compared three crystal structures of LASV GPC complexed with GPC-B antibodies of varying neutralization potency. Each GPC-B antibody recognized an overlapping epitope involved in binding of two adjacent GPC monomers and preserved the prefusion trimeric conformation. Differences among GPC-antibody interactions highlighted specific residues that enhance neutralization. Using structure-guided amino acid substitutions, we increased the neutralization potency and breadth of these antibodies to include all major LASV lineages. The ability to define antibody residues that allow potent and broad neutralizing activity, together with findings from analyses of inferred germline precursors, is critical to develop potent therapeutics and for vaccine design and assessment.
Keywords	epitopes ; neutralization ; germ cells ; antibody formation ; neutralization tests ; crystal structure ; amino acid substitution ; Lassa mammarenavirus ; therapeutics ; neutralizing antibodies ; vaccine development ; glycoproteins ; fever ; Western Africa
Language	English
Dates of publication	2019-0808
Size	p. 1004-1015.e14.
Publishing place	Elsevier Inc.
Document type	Article
Note	2019-12-06
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2019.07.020
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Article ; Online: Convergent Structures Illuminate Features for Germline Antibody Binding and Pan-Lassa Virus Neutralization.

Cell

2019 Volume 178, Issue 4, Page(s) 1004–1015.e14

Abstract	Lassa virus (LASV) causes hemorrhagic fever and is endemic in West Africa. Protective antibody responses primarily target the LASV surface glycoprotein (GPC), and GPC-B competition group antibodies often show potent neutralizing activity in humans. However, which features confer potent and broadly neutralizing antibody responses is unclear. Here, we compared three crystal structures of LASV GPC complexed with GPC-B antibodies of varying neutralization potency. Each GPC-B antibody recognized an overlapping epitope involved in binding of two adjacent GPC monomers and preserved the prefusion trimeric conformation. Differences among GPC-antibody interactions highlighted specific residues that enhance neutralization. Using structure-guided amino acid substitutions, we increased the neutralization potency and breadth of these antibodies to include all major LASV lineages. The ability to define antibody residues that allow potent and broad neutralizing activity, together with findings from analyses of inferred germline precursors, is critical to develop potent therapeutics and for vaccine design and assessment.
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Antigens, Viral/immunology ; Chlorocebus aethiops ; Drosophila/cytology ; Epitopes/chemistry ; Epitopes/immunology ; Germ Cells/immunology ; HEK293 Cells ; Humans ; Lassa Fever/immunology ; Lassa Fever/virology ; Lassa virus/immunology ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/immunology ; Protein Structure, Secondary ; Vero Cells ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/immunology ; Viral Vaccines/immunology
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Antigens, Viral ; Epitopes ; Membrane Glycoproteins ; Viral Envelope Proteins ; Viral Vaccines
Language	English
Publishing date	2019-08-14
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	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2019.07.020
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Article: Space-Time Trends in Lassa Fever in Sierra Leone by ELISA Serostatus, 2012-2019.

Microorganisms

2021 Volume 9, Issue 3

Abstract	Lassa fever (LF) is a viral hemorrhagic disease found in Sub-Saharan Africa and is responsible for up to 300,000 cases and 5000 deaths annually. LF is highly endemic in Sierra Leone, particularly in its Eastern Province. Kenema Government Hospital (KGH) maintains one of only a few LF isolation facilities in the world with year-round diagnostic testing. Here we focus on space-time trends for LF occurring in Sierra Leone between 2012 and 2019 to provide a current account of LF in the wake of the 2014-2016 Ebola epidemic. Data were analyzed for 3277 suspected LF cases and classified as acute, recent, and non-LF or prior LF exposure using enzyme-linked immunosorbent assays (ELISAs). Presentation rates for acute, recent, and non-LF or prior LF exposure were 6.0% (195/3277), 25.6% (838/3277), and 68.4% (2244/3277), respectively. Among 2051 non-LF or prior LF exposures, 33.2% (682/2051) tested positive for convalescent LF exposure. The overall LF case-fatality rate (CFR) was 78.5% (106/135). Both clinical presentations and confirmed LF cases declined following the Ebola epidemic. These declines coincided with an increased duration between illness onset and clinical presentation, perhaps suggesting more severe disease or presentation at later stages of illness. Acute LF cases and their corresponding CFRs peaked during the dry season (November to April). Subjects with recent (but not acute) LF exposure were more likely to present during the rainy season (May to October) than the dry season (
Language	English
Publishing date	2021-03-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms9030586
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Article ; Online: Structural basis for antibody-mediated neutralization of Lassa virus.

Hastie, Kathryn M / Zandonatti, Michelle A / Kleinfelter, Lara M / Heinrich, Megan L / Rowland, Megan M / Chandran, Kartik / Branco, Luis M / Robinson, James E / Garry, Robert F / Saphire, Erica Ollmann

Science (New York, N.Y.)

2017 Volume 356, Issue 6341, Page(s) 923–928

Abstract: The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here ... ...

Abstract	The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health.
MeSH term(s)	Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/chemistry ; Antibodies, Viral/metabolism ; Crystallization ; Epitopes/chemistry ; Humans ; Hydrogen-Ion Concentration ; Lassa Fever/immunology ; Lassa Fever/virology ; Lassa virus/chemistry ; Lassa virus/immunology ; Lassa virus/physiology ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Protein Stability ; Protein Structure, Quaternary ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism ; Virus Internalization
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Viral Envelope Proteins
Language	English
Publishing date	2017-06-01
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	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aam7260
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Article ; Online: Treatment of Lassa virus infection in outbred guinea pigs with first-in-class human monoclonal antibodies.

Cross, Robert W / Mire, Chad E / Branco, Luis M / Geisbert, Joan B / Rowland, Megan M / Heinrich, Megan L / Goba, Augustine / Momoh, Mambu / Grant, Donald S / Fullah, Mohamed / Khan, Sheik Humarr / Robinson, James E / Geisbert, Thomas W / Garry, Robert F

Antiviral research

2016 Volume 133, Page(s) 218–222

Abstract: Lassa fever is a significant health threat to West African human populations with hundreds of thousands of annual cases. There are no approved medical countermeasures currently available. Compassionate use of the antiviral drug ribavirin or transfusion ... ...

Abstract	Lassa fever is a significant health threat to West African human populations with hundreds of thousands of annual cases. There are no approved medical countermeasures currently available. Compassionate use of the antiviral drug ribavirin or transfusion of convalescent serum has resulted in mixed success depending on when administered or the donor source, respectively. We previously identified several recombinant human monoclonal antibodies targeting the glycoprotein of Lassa virus with strong neutralization profiles in vitro. Here, we demonstrate remarkable therapeutic efficacy using first-in-class human antibodies in a guinea pig model of Lassa infection thereby presenting a promising treatment alternative.
Language	English
Publishing date	2016-09
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	306628-9
ISSN	1872-9096 ; 0166-3542
ISSN (online)	1872-9096
ISSN	0166-3542
DOI	10.1016/j.antiviral.2016.08.012
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Article: Cross-Reactive Antibodies to SARS-CoV-2 and MERS-CoV in Pre-COVID-19 Blood Samples from Sierra Leoneans

Borrega, Rodrigo / Nelson, Diana K. S. / Koval, Anatoliy P. / Bond, Nell G. / Heinrich, Megan L. / Rowland, Megan M. / Lathigra, Raju / Bush, Duane J. / Aimukanova, Irina / Phinney, Whitney N. / Koval, Sophia A. / Hoffmann, Andrew R. / Smither, Allison R. / Bell-Kareem, Antoinette R. / Melnik, Lilia I. / Genemaras, Kaylynn J. / Chao, Karissa / Snarski, Patricia / Melton, Alexandra B. /

Viruses. 2021 Nov. 21, v. 13, no. 11

2021

Abstract: Many countries in sub-Saharan Africa have experienced lower COVID-19 caseloads and fewer deaths than countries in other regions worldwide. Under-reporting of cases and a younger population could partly account for these differences, but pre-existing ... ...

Abstract	Many countries in sub-Saharan Africa have experienced lower COVID-19 caseloads and fewer deaths than countries in other regions worldwide. Under-reporting of cases and a younger population could partly account for these differences, but pre-existing immunity to coronaviruses is another potential factor. Blood samples from Sierra Leonean Lassa fever and Ebola survivors and their contacts collected before the first reported COVID-19 cases were assessed using enzyme-linked immunosorbent assays for the presence of antibodies binding to proteins of coronaviruses that infect humans. Results were compared to COVID-19 subjects and healthy blood donors from the United States. Prior to the pandemic, Sierra Leoneans had more frequent exposures than Americans to coronaviruses with epitopes that cross-react with severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), SARS-CoV, and Middle Eastern respiratory syndrome coronavirus (MERS-CoV). The percentage of Sierra Leoneans with antibodies reacting to seasonal coronaviruses was also higher than for American blood donors. Serological responses to coronaviruses by Sierra Leoneans did not differ by age or sex. Approximately a quarter of Sierra Leonian pre-pandemic blood samples had neutralizing antibodies against SARS-CoV-2 pseudovirus, while about a third neutralized MERS-CoV pseudovirus. Prior exposures to coronaviruses that induce cross-protective immunity may contribute to reduced COVID-19 cases and deaths in Sierra Leone.
Keywords	COVID-19 infection ; Lassa virus fever ; Pseudovirus ; Severe acute respiratory syndrome coronavirus 2 ; blood ; cross immunity ; epitopes ; pandemic ; Sierra Leone
Language	English
Dates of publication	2021-1121
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13112325
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Article ; Online: Human-monoclonal-antibody therapy protects nonhuman primates against advanced Lassa fever.

Mire, Chad E / Cross, Robert W / Geisbert, Joan B / Borisevich, Viktoriya / Agans, Krystle N / Deer, Daniel J / Heinrich, Megan L / Rowland, Megan M / Goba, Augustine / Momoh, Mambu / Boisen, Mathew L / Grant, Donald S / Fullah, Mohamed / Khan, Sheik Humarr / Fenton, Karla A / Robinson, James E / Branco, Luis M / Garry, Robert F / Geisbert, Thomas W

Nature medicine

2017 Volume 23, Issue 10, Page(s) 1146–1149

Abstract: There are no approved treatments for Lassa fever, which is endemic to the same regions of West Africa that were recently devastated by Ebola. Here we show that a combination of human monoclonal antibodies that cross-react with the glycoproteins of all ... ...

Abstract	There are no approved treatments for Lassa fever, which is endemic to the same regions of West Africa that were recently devastated by Ebola. Here we show that a combination of human monoclonal antibodies that cross-react with the glycoproteins of all four clades of Lassa virus is able to rescue 100% of cynomolgus macaques when treatment is initiated at advanced stages of disease, including up to 8 d after challenge.
MeSH term(s)	Animals ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Neutralizing/therapeutic use ; Antibodies, Viral/therapeutic use ; Cross Reactions ; Enzyme-Linked Immunosorbent Assay ; Humans ; Immune Evasion/genetics ; Immunohistochemistry ; Lassa Fever/prevention & control ; Lassa virus/genetics ; Macaca fascicularis ; RNA, Viral/blood ; Random Allocation ; Survival Rate ; Viral Load
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; RNA, Viral
Language	English
Publishing date	2017-09-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/nm.4396
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