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Article ; Online: Ebola Virus Infection Induces HCAR2 Expression Leading to Cell Death.

Kuroda, Makoto / Halfmann, Peter J / Kawaoka, Yoshihiro

2023 Volume 228, Issue Suppl 7, Page(s) S508–S513

Abstract: Ebola virus (EBOV) induces cell death not only in infected permissive cells but also in nonpermissive, bystander cells by employing different mechanisms. Hydroxycarboxylic acid receptor 2 (HCAR2) has been reported to be involved in apoptotic cell death. ... ...

Abstract	Ebola virus (EBOV) induces cell death not only in infected permissive cells but also in nonpermissive, bystander cells by employing different mechanisms. Hydroxycarboxylic acid receptor 2 (HCAR2) has been reported to be involved in apoptotic cell death. We previously reported an increase in the expression of HCAR2-specific mRNA in EBOV-infected individuals with fatal outcomes. Here, we report that infection with an EBOV lacking the VP30 gene (EBOVΔVP30) results in the upregulation of HCAR2 mRNA expression in human hepatocyte Huh7.0 cells stably expressing VP30. Transient overexpression of HCAR2 reduced the viability of Huh7.0 cells and human embryonic kidney cells. Phosphatidylserine externalization and cell membrane permeabilization by HCAR2 overexpression was also observed. Interestingly, coexpression of HCAR2 with EBOV VP40 further reduced cell viability in transfected cells compared to HCAR2 coexpression with other viral proteins. Our data suggest that HCAR2 may contribute to EBOV-induced cell death.
MeSH term(s)	Humans ; Cell Death ; Ebolavirus/physiology ; Hemorrhagic Fever, Ebola ; RNA, Messenger/metabolism ; Viral Proteins/metabolism
Chemical Substances	RNA, Messenger ; Viral Proteins ; HCAR2 protein, human
Language	English
Publishing date	2023-09-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiad344
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Article ; Online: An Antiviral Role for TRIM14 in Ebola Virus Infection.

Kuroda, Makoto / Halfmann, Peter J / Thackray, Larissa B / Diamond, Michael S / Feldmann, Heinz / Marzi, Andrea / Kawaoka, Yoshihiro

The Journal of infectious diseases

2024 Volume 228, Issue Suppl 7, Page(s) S514–S521

Abstract: Ebola virus (EBOV) is a highly pathogenic virus that encodes 7 multifunctional structural proteins. Multiple host factors have been reported to interact with the EBOV proteins. Here, we found that tripartite motif-containing 14 (TRIM14), an interferon- ... ...

Abstract	Ebola virus (EBOV) is a highly pathogenic virus that encodes 7 multifunctional structural proteins. Multiple host factors have been reported to interact with the EBOV proteins. Here, we found that tripartite motif-containing 14 (TRIM14), an interferon-stimulated gene that mediates cellular signaling pathways associated with type I interferon and inflammatory cytokine production, interacts with EBOV nucleoprotein to enhance interferon-β (IFN-β) and nuclear factor-κB (NF-κB) promotor activation. Moreover, TRIM14 overexpression reduced viral replication in an infectious but biologically contained EBOVΔVP30 system by approximately 10-fold without affecting viral protein expression. Furthermore, TRM14-deficient mice were more susceptible to mouse-adapted EBOV infection than wild-type mice. Our data suggest that TRIM14 is a host factor with anti-EBOV activity that limits EBOV pathogenesis.
MeSH term(s)	Animals ; Mice ; Ebolavirus/genetics ; Hemorrhagic Fever, Ebola ; Interferon Type I/metabolism ; Viral Proteins/metabolism
Chemical Substances	Interferon Type I ; Viral Proteins ; Trim14 protein, mouse
Language	English
Publishing date	2024-02-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiad325
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Article ; Online: Broad protection against clade 1 sarbecoviruses after a single immunization with cocktail spike-protein-nanoparticle vaccine.

Halfmann, Peter J / Loeffler, Kathryn / Duffy, Augustine / Kuroda, Makoto / Yang, Jie E / Wright, Elizabeth R / Kawaoka, Yoshihiro / Kane, Ravi S

Nature communications

2024 Volume 15, Issue 1, Page(s) 1284

Abstract: The 2002 SARS outbreak, the 2019 emergence of COVID-19, and the continuing evolution of immune-evading SARS-CoV-2 variants together highlight the need for a broadly protective vaccine against ACE2-utilizing sarbecoviruses. While updated variant-matched ... ...

Abstract	The 2002 SARS outbreak, the 2019 emergence of COVID-19, and the continuing evolution of immune-evading SARS-CoV-2 variants together highlight the need for a broadly protective vaccine against ACE2-utilizing sarbecoviruses. While updated variant-matched formulations are a step in the right direction, protection needs to extend beyond SARS-CoV-2 and its variants to include SARS-like viruses. Here, we introduce bivalent and trivalent vaccine formulations using our spike protein nanoparticle platform that completely protect female hamsters against BA.5 and XBB.1 challenges with no detectable virus in the lungs. The trivalent cocktails elicit highly neutralizing responses against all tested Omicron variants and the bat sarbecoviruses SHC014 and WIV1. Finally, our 614D/SHC014/XBB trivalent spike formulation completely protects human ACE2-transgenic female hamsters against challenges with WIV1 and SHC014 with no detectable virus in the lungs. Collectively, these results illustrate that our trivalent protein-nanoparticle cocktail can provide broad protection against SARS-CoV-2-like and SARS-CoV-1-like sarbecoviruses.
MeSH term(s)	Animals ; Cricetinae ; Humans ; Female ; Nanovaccines ; Severe acute respiratory syndrome-related coronavirus ; Angiotensin-Converting Enzyme 2 ; Vaccination ; Immunization ; Antibodies, Neutralizing ; Antibodies, Viral
Chemical Substances	Nanovaccines ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Antibodies, Neutralizing ; Antibodies, Viral
Language	English
Publishing date	2024-02-12
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-45495-6
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Article: Broad Protection Against Clade 1 Sarbecoviruses After a Single Immunization with Cocktail Spike-Protein-Nanoparticle Vaccine.

Halfmann, Peter J / Loeffler, Kathryn / Duffy, Augustine / Kuroda, Makoto / Kawaoka, Yoshihiro / Kane, Ravi S

Research square

2023

Abstract	The 2002 SARS outbreak, the 2019 emergence of COVID-19, and the continuing evolution of immune-evading SARS-CoV-2 variants together highlight the need for a broadly protective vaccine against ACE2-utilizing sarbecoviruses. While updated variant-matched formulations such as Pfizer-BioNTech's bivalent vaccine are a step in the right direction, protection needs to extend beyond SARS-CoV-2 and its variants to include SARS-like viruses. Here, we introduce bivalent and trivalent vaccine formulations using our spike protein nanoparticle platform that completely protected hamsters against BA.5 and XBB.1 challenges with no detectable virus in the lungs. The trivalent cocktails elicited highly neutralizing responses against all tested Omicron variants and the bat sarbecoviruses SHC014 and WIV1. Finally, our 614D/SHC014/XBB trivalent spike formulation completely protected human ACE2-transgenic hamsters against challenges with WIV1 and SHC014 with no detectable virus in the lungs. Collectively, these results illustrate that our trivalent protein-nanoparticle cocktail can provide broad protection against SARS-CoV-2-like and SARS-CoV-1-like sarbecoviruses.
Language	English
Publishing date	2023-06-29
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-3088907/v1
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Article ; Online: Replicative capacity of SARS-CoV-2 omicron variants BA.5 and BQ.1.1 at elevated temperatures.

Muramoto, Yukiko / Takahashi, Senye / Halfmann, Peter J / Gotoh, Shimpei / Noda, Takeshi / Kawaoka, Yoshihiro

The Lancet. Microbe

2023 Volume 4, Issue 7, Page(s) e486

MeSH term(s)	Humans ; COVID-19 ; SARS-CoV-2/genetics ; Temperature
Language	English
Publishing date	2023-04-24
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2666-5247
ISSN (online)	2666-5247
DOI	10.1016/S2666-5247(23)00100-3
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Article ; Online: HER2-mediated enhancement of Ebola virus entry.

Kuroda, Makoto / Halfmann, Peter / Kawaoka, Yoshihiro

PLoS pathogens

2020 Volume 16, Issue 10, Page(s) e1008900

Abstract: Multiple cell surface molecules including TAM receptors (TYRO3, AXL, and MERTK), a family of tyrosine kinase receptors, can serve as attachment receptors for Ebola virus (EBOV) entry into cells. The interaction of these receptors with EBOV particles is ... ...

Abstract	Multiple cell surface molecules including TAM receptors (TYRO3, AXL, and MERTK), a family of tyrosine kinase receptors, can serve as attachment receptors for Ebola virus (EBOV) entry into cells. The interaction of these receptors with EBOV particles is believed to trigger the initial internalization events that lead to macropinocytosis. However, the details of how these interactions lead to EBOV internalization have yet to be elucidated. Here, we screened receptor tyrosine kinase (RTK) inhibitors for anti-EBOV activity by using our previously established biologically contained Ebola virus that lacks the VP30 gene (EBOVΔVP30) and identified several RTKs, including human epidermal growth factor receptor 2 (HER2), as potential targets of anti-EBOV inhibitors and as novel host factors that have a role in EBOV infection. Of these identified RTKs, it was only HER2 whose knockdown by siRNAs impaired EBOVΔVP30-induced AKT1 phosphorylation, an event that is required for AKT1 activation and subsequent macropinocytosis. Stable expression of HER2 resulted in constitutive activation of AKT1, resulting in the enhancement of EBOVΔVP30 growth, EBOV GP-mediated entry, and macropinocytosis. Moreover, we found that HER2 interacts with the TAM receptors, and in particular forms a complex with TYRO3 and EBOVΔVP30 particles on the cell surface. Interestingly, HER2 was required for EBOVΔVP30-induced TYRO3 and AKT1 activation, but the other TAM receptors (TYRO3 and MERTK) were not essential for EBOVΔVP30-induced HER2 and AKT1 activation. Our findings demonstrate that HER2 plays an important role in EBOV entry and provide novel insights for the development of therapeutics against the virus.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Chlorocebus aethiops ; Ebolavirus/genetics ; Ebolavirus/pathogenicity ; HEK293 Cells ; Hemorrhagic Fever, Ebola/virology ; Humans ; Membrane Glycoproteins/metabolism ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, ErbB-2/metabolism ; Vero Cells/virology ; Virus Internalization/drug effects
Chemical Substances	Carrier Proteins ; Membrane Glycoproteins ; ERBB2 protein, human (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1)
Language	English
Publishing date	2020-10-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1008900
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Article ; Online: Comparative Sensitivity of Rapid Antigen Tests for the Delta Variant (B.1.617.2) of SARS-CoV-2.

Sakai-Tagawa, Yuko / Yamayoshi, Seiya / Halfmann, Peter J / Kawaoka, Yoshihiro

Viruses

2021 Volume 13, Issue 11

Abstract: Rapid antigen tests (RATs) for COVID-19 based on lateral flow immunoassays are useful for rapid diagnosis in a variety of settings. Although many kinds of RATs are available, their respective sensitivity has not been compared. Here, we examined the ... ...

Abstract	Rapid antigen tests (RATs) for COVID-19 based on lateral flow immunoassays are useful for rapid diagnosis in a variety of settings. Although many kinds of RATs are available, their respective sensitivity has not been compared. Here, we examined the sensitivity of 27 RATs available in Japan for the detection of the SARS-CoV-2 delta variant. All of the RATs tested detected the delta variant albeit with different sensitivities. Nine RATs (ESPLINE SARS-CoV-2, ALSONIC COVID-19 Ag, COVID-19 and Influenza A+B Antigen Combo Rapid Test, ImmunoArrow SARS-CoV-2, Fuji Dri-chem immuno AG cartridge COVID-19 Ag, 2019-nCoV Ag rapid detection kit, Saliva SARS-CoV-2(2019-nCoV) Antigen Test Kit, and Rabliss SARS-CoV-2 antigen detection kit COVID19 AG) showed superior sensitivity to the isolated delta variant. Although actual clinical specimens were not examined, the detection level of most of the RATs was 7500 pfu, indicating that individuals whose test samples contained less virus than that would be considered negative. Therefore, it is important to bear in mind that RATs may miss individuals shedding low levels of infectious virus.
MeSH term(s)	Antigens, Viral/analysis ; COVID-19/diagnosis ; COVID-19/virology ; COVID-19 Serological Testing ; Humans ; Immunoassay ; Reagent Strips ; SARS-CoV-2/immunology ; SARS-CoV-2/isolation & purification ; Sensitivity and Specificity
Chemical Substances	Antigens, Viral ; Reagent Strips
Language	English
Publishing date	2021-10-29
Publishing country	Switzerland
Document type	Comparative Study ; Evaluation Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13112183
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Article ; Online: The Mucin-Like Domain of the Ebola Glycoprotein Does Not Impact Virulence or Pathogenicity in Ferrets.

Halfmann, Peter J / Borisevich, Viktoriya / Levine, Corri B / Mire, Chad E / Fenton, Karla A / Geisbert, Thomas W / Kawaoka, Yoshihiro / Cross, Robert W

The Journal of infectious diseases

2023 Volume 228, Issue Suppl 7, Page(s) S587–S593

Abstract: Background: Ebola virus (EBOV) is considered among the most dangerous viruses with case fatality rates approaching 90% depending on the outbreak. While several viral proteins (VPs) including VP24, VP35, and the soluble glycoprotein are understood to ... ...

Abstract	Background: Ebola virus (EBOV) is considered among the most dangerous viruses with case fatality rates approaching 90% depending on the outbreak. While several viral proteins (VPs) including VP24, VP35, and the soluble glycoprotein are understood to contribute to virulence, less is known of the contribution of the highly variable mucin-like domain (MLD) of EBOV. Early studies have defined a potential role in immune evasion of the MLD by providing a glycan shield to critical glycoprotein residues tied to viral entry. Nonetheless, little is known as to what direct role the MLD plays in acute EBOV disease (EVD). Methods: We generated an infectious EBOV clone that lacks the MLD and assessed its virulence in ferrets compared with wild-type (WT) virus. Results: No differences in growth kinetics were observed in vitro, nor were there any differences in time to death, viremia, or clinical picture in ferrets infected with recombinant EBOV (rEBOV)-WT or rEBOV-Δmucin. Conclusions: The EBOV MLD does not play a critical role in acute pathogenesis of EVD in ferrets.
MeSH term(s)	Animals ; Humans ; Hemorrhagic Fever, Ebola ; Mucins ; Virulence ; Ferrets ; Ebolavirus ; Glycoproteins/genetics ; Glycoproteins/metabolism
Chemical Substances	Mucins ; Glycoproteins
Language	English
Publishing date	2023-06-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiad240
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Article ; Online: Transmission and re-infection of Omicron variant XBB.1.5 in hamsters.

Halfmann, Peter J / Uraki, Ryuta / Kuroda, Makoto / Iwatsuki-Horimoto, Kiyoko / Yamayoshi, Seiya / Ito, Mutsumi / Kawaoka, Yoshihiro

EBioMedicine

2023 Volume 93, Page(s) 104677

Abstract: Background: Like its predecessors in the XBB family, XBB.1.5 is highly immune evasive from therapeutic monoclonal antibodies and neutralizing antibodies generated by vaccination and/or infection. However, there is a lack of in vivo data on XBB.1.5 in ... ...

Abstract	Background: Like its predecessors in the XBB family, XBB.1.5 is highly immune evasive from therapeutic monoclonal antibodies and neutralizing antibodies generated by vaccination and/or infection. However, there is a lack of in vivo data on XBB.1.5 in animal models such as Syrian hamsters. Methods: Syrian hamsters (females) were used to examine airborne transmission along with virus replication of XBB.1.5 in naïve animals and human ACE2 hamsters with pre-existing immunity from a previous infection with Omicron BA.1. Assays were performed to determine neutralizing antibody responses, and virus titers were determined by standard plaque assays. Findings: Unlike earlier Omicron subvariants, such as BA.1 and BA.2, XBB.1.5 transmitted more efficiently in the hamster model. In addition, XBB.1.5 partially escaped BA.1-immunity from a previous infection with XBB.1.5 replicating in the nasal turbinate tissues and to a lesser extend in the lung tissues of previously infected hamsters. Interpretation: Our in vivo data showing better airborne transmissibility of the Omicron subvariant XBB.1.5 than its predecessor, BA.2, in Syrian hamsters will allow researchers to further investigate amino acid substitutions that give XBB.1.5 a fitness advantage over BA.2 in transmission, data that may be important in studies of SARS-CoV-2 transmission in humans. Funding: This research is supported by grants from the Center for Research on Influenza Pathogenesis and Transmission (CRIPT; 75N93021C00014), funded by the National Institute of Allergy and Infectious Diseases and by a Research Program on Emerging and Reemerging Infectious Diseases (JP21fk0108552 and JP21fk0108615), a Project Promoting Support for Drug Discovery (JP21nf0101632), the Japan Program for Infectious Diseases Research and Infrastructure (JP22wm0125002), and The University of Tokyo Pandemic Preparedness, Infection and Advanced Research Center (UTOPIA) grant (JP223fa627001) from the Japan Agency for Medical Research and Development.
MeSH term(s)	Animals ; Female ; Cricetinae ; Humans ; Reinfection ; COVID-19 ; Mesocricetus ; SARS-CoV-2 ; Antibodies, Neutralizing ; Adaptor Proteins, Signal Transducing
Chemical Substances	Antibodies, Neutralizing ; CRIPT protein, human ; Adaptor Proteins, Signal Transducing
Language	English
Publishing date	2023-06-21
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2023.104677
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Article ; Online: Characterization of highly pathogenic clade 2.3.4.4b H5N1 mink influenza viruses.

Maemura, Tadashi / Guan, Lizheng / Gu, Chunyang / Eisfeld, Amie / Biswas, Asim / Halfmann, Peter / Neumann, Gabriele / Kawaoka, Yoshihiro

EBioMedicine

2023 Volume 97, Page(s) 104827

Language	English
Publishing date	2023-10-07
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2023.104827
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