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Article ; Online: Broadly Protective Neuraminidase-Based Influenza Vaccines and Monoclonal Antibodies: Target Epitopes and Mechanisms of Action.

Abbadi, Nada / Mousa, Jarrod J

2023 Volume 15, Issue 1

Abstract: Neuraminidase (NA) is an important surface protein on influenza virions, playing an essential role in the viral life cycle and being a key target of the immune system. Despite the importance of NA-based immunity, current vaccines are focused on the ... ...

Abstract	Neuraminidase (NA) is an important surface protein on influenza virions, playing an essential role in the viral life cycle and being a key target of the immune system. Despite the importance of NA-based immunity, current vaccines are focused on the hemagglutinin (HA) protein as the target for protective antibodies, and the amount of NA is not standardized in virion-based vaccines. Antibodies targeting NA are predominantly protective, reducing infection severity and viral shedding. Recently, NA-specific monoclonal antibodies have been characterized, and their target epitopes have been identified. This review summarizes the characteristics of NA, NA-specific antibodies, the mechanism of NA inhibition, and the recent efforts towards developing NA-based and NA-incorporating influenza vaccines.
MeSH term(s)	Humans ; Influenza Vaccines ; Neuraminidase ; Antibodies, Monoclonal ; Antibodies, Viral ; Influenza, Human/prevention & control ; Hemagglutinin Glycoproteins, Influenza Virus ; Orthomyxoviridae Infections
Chemical Substances	Influenza Vaccines ; Neuraminidase (EC 3.2.1.18) ; Antibodies, Monoclonal ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus
Language	English
Publishing date	2023-01-10
Publishing country	Switzerland
Document type	Review ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v15010200
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Epitope Binning of Monoclonal and Polyclonal Antibodies by Biolayer Interferometry.

Nagashima, Kaito / Mousa, Jarrod J

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2673, Page(s) 17–32

Abstract: Understanding the epitopes of antibodies elicited by infection and vaccination is often useful in immunogen design. In this chapter, we describe biolayer interferometry (BLI)-based methods to evaluate such epitopes and permit simultaneous analysis of ... ...

Abstract	Understanding the epitopes of antibodies elicited by infection and vaccination is often useful in immunogen design. In this chapter, we describe biolayer interferometry (BLI)-based methods to evaluate such epitopes and permit simultaneous analysis of antibodies from several sources, including monoclonal antibodies (mAbs) and polyclonal serum antibodies (pAbs). Using previously characterized antibodies with known epitopes as controls, the distribution of epitopes for the influenza hemagglutinin (HA) is shown for isolated human mAbs and pooled serum from HA-immunized mice. This method is versatile, high-throughput, and can be adapted to several antigens.
MeSH term(s)	Humans ; Animals ; Mice ; Epitopes ; Antibodies, Monoclonal ; Influenza, Human ; Hemagglutinins ; Interferometry/methods ; Antibodies, Viral ; Epitope Mapping/methods ; Hemagglutinin Glycoproteins, Influenza Virus
Chemical Substances	Epitopes ; Antibodies, Monoclonal ; Hemagglutinins ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus
Language	English
Publishing date	2023-05-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3239-0_2
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Article ; Online: Structural basis for respiratory syncytial virus and human metapneumovirus neutralization.

Miller, Rose J / Mousa, Jarrod J

Current opinion in virology

2023 Volume 61, Page(s) 101337

Abstract: Respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) continue to be a global burden to infants, the elderly, and immunocompromised individuals. In the past ten years, there has been substantial progress in the development of new vaccine ... ...

Abstract	Respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) continue to be a global burden to infants, the elderly, and immunocompromised individuals. In the past ten years, there has been substantial progress in the development of new vaccine candidates and therapies against these viruses. These advancements were guided by the structural elucidation of the major surface glycoproteins for these viruses, the fusion (F) protein and attachment (G) protein. The identification of immunodominant epitopes on the RSV F and hMPV F proteins has expanded current knowledge on antibody-mediated immune responses, which has led to new approaches for vaccine and therapeutic development through the stabilization of pre-fusion constructs of the F protein and pre-fusion-specific monoclonal antibodies with high potency and efficacy. In this review, we describe structural characteristics of known antigenic sites on the RSV and hMPV proteins, their influence on the immune response, and current progress in vaccine and therapeutic development.
MeSH term(s)	Humans ; Aged ; Metapneumovirus/metabolism ; Antibodies, Viral ; Antibodies, Neutralizing ; Viral Fusion Proteins/chemistry ; Respiratory Syncytial Virus, Human ; Respiratory Syncytial Virus Infections/prevention & control
Chemical Substances	Antibodies, Viral ; Antibodies, Neutralizing ; Viral Fusion Proteins
Language	English
Publishing date	2023-08-05
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2611378-8
ISSN	1879-6265 ; 1879-6257
ISSN (online)	1879-6265
ISSN	1879-6257
DOI	10.1016/j.coviro.2023.101337
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Article ; Online: Diverse Mechanisms of Protective Anti-Pneumococcal Antibodies.

Gingerich, Aaron D / Mousa, Jarrod J

Frontiers in cellular and infection microbiology

2022 Volume 12, Page(s) 824788

Abstract: The gram-positive ... ...

Abstract	The gram-positive bacterium
MeSH term(s)	Adult ; Antibodies, Bacterial ; Child ; Humans ; Pneumococcal Infections/microbiology ; Pneumococcal Vaccines ; Streptococcus pneumoniae/genetics ; Vaccines, Conjugate
Chemical Substances	Antibodies, Bacterial ; Pneumococcal Vaccines ; Vaccines, Conjugate
Language	English
Publishing date	2022-01-28
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.824788
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Article ; Online: Next-Generation Influenza HA Immunogens and Adjuvants in Pursuit of a Broadly Protective Vaccine.

Nagashima, Kaito A / Mousa, Jarrod J

Viruses

2021 Volume 13, Issue 4

Abstract: Influenza virus, a highly mutable respiratory pathogen, causes significant disease nearly every year. Current vaccines are designed to protect against circulating influenza strains of a given season. However, mismatches between vaccine strains and ... ...

Abstract	Influenza virus, a highly mutable respiratory pathogen, causes significant disease nearly every year. Current vaccines are designed to protect against circulating influenza strains of a given season. However, mismatches between vaccine strains and circulating strains, as well as inferior vaccine effectiveness in immunodeficient populations, represent major obstacles. In an effort to expand the breadth of protection elicited by influenza vaccination, one of the major surface glycoproteins, hemagglutinin (HA), has been modified to develop immunogens that display conserved regions from multiple viruses or elicit a highly polyclonal antibody response to broaden protection. These approaches, which target either the head or the stalk domain of HA, or both domains, have shown promise in recent preclinical and clinical studies. Furthermore, the role of adjuvants in bolstering the robustness of the humoral response has been studied, and their effects on the vaccine-elicited antibody repertoire are currently being investigated. This review will discuss the progress made in the universal influenza vaccine field with respect to influenza A viruses from the perspectives of both antigen and adjuvant, with a focus on the elicitation of broadly neutralizing antibodies.
MeSH term(s)	Adjuvants, Immunologic ; Animals ; Antibodies, Viral/immunology ; Clinical Trials as Topic ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Immunity, Humoral ; Influenza A virus/immunology ; Influenza Vaccines/genetics ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Mice ; Orthomyxoviridae Infections/immunology ; Orthomyxoviridae Infections/prevention & control ; Orthomyxoviridae Infections/virology ; Vaccines, Virus-Like Particle/immunology
Chemical Substances	Adjuvants, Immunologic ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Influenza Vaccines ; Vaccines, Virus-Like Particle
Language	English
Publishing date	2021-03-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13040546
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Article ; Online: Structural basis of the amidase ClbL central to the biosynthesis of the genotoxin colibactin.

Tripathi, Prabhanshu / Mousa, Jarrod J / Guntaka, Naga Sandhya / Bruner, Steven D

Acta crystallographica. Section D, Structural biology

2023 Volume 79, Issue Pt 9, Page(s) 830–836

Abstract: Colibactin is a genotoxic natural product produced by select commensal bacteria in the human gut microbiota. The compound is a bis-electrophile that is predicted to form interstrand DNA cross-links in target cells, leading to double-strand DNA breaks. ... ...

Abstract	Colibactin is a genotoxic natural product produced by select commensal bacteria in the human gut microbiota. The compound is a bis-electrophile that is predicted to form interstrand DNA cross-links in target cells, leading to double-strand DNA breaks. The biosynthesis of colibactin is carried out by a mixed NRPS-PKS assembly line with several noncanonical features. An amidase, ClbL, plays a key role in the pathway, catalyzing the final step in the formation of the pseudodimeric scaffold. ClbL couples α-aminoketone and β-ketothioester intermediates attached to separate carrier domains on the NRPS-PKS assembly. Here, the 1.9 Å resolution structure of ClbL is reported, providing a structural basis for this key step in the colibactin biosynthetic pathway. The structure reveals an open hydrophobic active site surrounded by flexible loops, and comparison with homologous amidases supports its unusual function and predicts macromolecular interactions with pathway carrier-protein substrates. Modeling protein-protein interactions supports a predicted molecular basis for enzyme-carrier domain interactions. Overall, the work provides structural insight into this unique enzyme that is central to the biosynthesis of colibactin.
MeSH term(s)	Humans ; Mutagens/metabolism ; Escherichia coli/genetics ; Amidohydrolases
Chemical Substances	colibactin ; Mutagens ; amidase (EC 3.5.1.4) ; Amidohydrolases (EC 3.5.-)
Language	English
Publishing date	2023-08-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2968623-4
ISSN	2059-7983 ; 0907-4449
ISSN (online)	2059-7983
ISSN	0907-4449
DOI	10.1107/S2059798323005703
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Article ; Online: A Pan-Pneumovirus vaccine based on immunodominant epitopes of the fusion protein.

Huang, Jiachen / Miller, Rose J / Mousa, Jarrod J

Frontiers in immunology

2022 Volume 13, Page(s) 941865

Abstract: Respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are two leading causes of severe respiratory infections in children, the elderly, and immunocompromised patients. The fusion (F) protein is the major target of neutralizing antibodies. ... ...

Abstract	Respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are two leading causes of severe respiratory infections in children, the elderly, and immunocompromised patients. The fusion (F) protein is the major target of neutralizing antibodies. Recent developments in stabilizing the pre-fusion conformation of the F proteins, and identifying immunodominant epitopes that elicit potent neutralizing antibodies have led to the testing of numerous pre-fusion RSV F-based vaccines in clinical trials. We designed and tested the immunogenicity and protective efficacy of a chimeric fusion protein that contains immunodominant epitopes of RSV F and hMPV F (RHMS-1). RHMS-1 has several advantages over vaccination with pre-fusion RSV F or hMPV F, including a focus on recalling B cells to the most important protective epitopes and the ability to induce protection against two viruses with a single antigen. RHMS-1 was generated as a trimeric recombinant protein, and analysis by negative-stain electron microscopy demonstrated the protein resembles the pre-fusion conformation. Probing of RHMS-1 antigenicity using a panel of RSV and hMPV F-specific monoclonal antibodies (mAbs) revealed the protein retains features of both viruses, including the pre-fusion site Ø epitope of RSV F. Mice immunized with RHMS-1 generated neutralizing antibodies to both viruses and were completely protected from RSV or hMPV challenge. Overall, this study demonstrates protection against two viruses with a single antigen and supports testing of RHMS-1 in additional pre-clinical animal models.
MeSH term(s)	Aged ; Animals ; Antibodies, Neutralizing ; Antibodies, Viral ; Child ; Epitopes ; Humans ; Immunodominant Epitopes/genetics ; Metapneumovirus/genetics ; Mice ; Recombinant Proteins ; Respiratory Syncytial Virus Vaccines ; Respiratory Syncytial Virus, Human/genetics ; Viral Fusion Proteins/genetics ; Viral Vaccines/genetics
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Immunodominant Epitopes ; Recombinant Proteins ; Respiratory Syncytial Virus Vaccines ; Viral Fusion Proteins ; Viral Vaccines
Language	English
Publishing date	2022-08-08
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.941865
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Article: Pneumocystis

Gingerich, Aaron D / Norris, Karen A / Mousa, Jarrod J

Pathogens (Basel, Switzerland)

2021 Volume 10, Issue 2

Abstract: For individuals who are immunocompromised, the opportunistic fungal ... ...

Abstract	For individuals who are immunocompromised, the opportunistic fungal pathogen
Language	English
Publishing date	2021-02-19
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2695572-6
ISSN	2076-0817
ISSN	2076-0817
DOI	10.3390/pathogens10020236
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Article ; Online: Adjuvant-Mediated Differences in Antibody Responses to Computationally Optimized Hemagglutinin and Neuraminidase Vaccines.

Nagashima, Kaito / Abbadi, Nada / Vyas, Ved / Roegner, Abigail / Ross, Ted M / Mousa, Jarrod J

Viruses

2023 Volume 15, Issue 2

Abstract: Computationally optimized broadly reactive antigens (COBRAs) are a next-generation universal influenza vaccine candidate. However, how these COBRAs induce antibody responses when combined with different adjuvants has not previously been well- ... ...

Abstract	Computationally optimized broadly reactive antigens (COBRAs) are a next-generation universal influenza vaccine candidate. However, how these COBRAs induce antibody responses when combined with different adjuvants has not previously been well-characterized. Therefore, we performed in vivo studies with an HA-based H1 COBRA, Y2, and an NA-based N1 COBRA, N1-I, to assess this effect for the H1N1 subtype. We tested the adjuvants AddaVax, AddaS03, CpG, and Alhydrogel. AddaS03 performed the best, eliciting high IgG titers and hemagglutination inhibition (HAI) activity for Y2 immunizations. Interestingly, serum antibody epitopes were relatively similar across adjuvant groups. Moreover, following N1-I immunization with these adjuvants, AddaS03 also elicited the highest IgG and neuraminidase inhibition (NAI) titers against the 2009 pandemic virus, A/California/07/2009 (A/CA/09). These results inform adjuvant selection efforts for H1 and N1 COBRA HA and NA antigens in a mouse model.
MeSH term(s)	Animals ; Mice ; Hemagglutinins ; Neuraminidase ; Antibody Formation ; Influenza A Virus, H1N1 Subtype ; Adjuvants, Immunologic ; Influenza Vaccines ; Immunoglobulin G
Chemical Substances	Hemagglutinins ; Neuraminidase (EC 3.2.1.18) ; Adjuvants, Immunologic ; Influenza Vaccines ; Immunoglobulin G
Language	English
Publishing date	2023-01-25
Publishing country	Switzerland
Document type	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/v15020347
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Article ; Online: A general computational design strategy for stabilizing viral class I fusion proteins.

Gonzalez, Karen J / Huang, Jiachen / Criado, Miria F / Banerjee, Avik / Tompkins, Stephen M / Mousa, Jarrod J / Strauch, Eva-Maria

Nature communications

2024 Volume 15, Issue 1, Page(s) 1335

Abstract: Many pathogenic viruses rely on class I fusion proteins to fuse their viral membrane with the host cell membrane. To drive the fusion process, class I fusion proteins undergo an irreversible conformational change from a metastable prefusion state to an ... ...

Abstract	Many pathogenic viruses rely on class I fusion proteins to fuse their viral membrane with the host cell membrane. To drive the fusion process, class I fusion proteins undergo an irreversible conformational change from a metastable prefusion state to an energetically more stable postfusion state. Mounting evidence underscores that antibodies targeting the prefusion conformation are the most potent, making it a compelling vaccine candidate. Here, we establish a computational design protocol that stabilizes the prefusion state while destabilizing the postfusion conformation. With this protocol, we stabilize the fusion proteins of the RSV, hMPV, and SARS-CoV-2 viruses, testing fewer than a handful of designs. The solved structures of these designed proteins from all three viruses evidence the atomic accuracy of our approach. Furthermore, the humoral response of the redesigned RSV F protein compares to that of the recently approved vaccine in a mouse model. While the parallel design of two conformations allows the identification of energetically sub-optimal positions for one conformation, our protocol also reveals diverse molecular strategies for stabilization. Given the clinical significance of viruses using class I fusion proteins, our algorithm can substantially contribute to vaccine development by reducing the time and resources needed to optimize these immunogens.
MeSH term(s)	Animals ; Mice ; Viral Fusion Proteins ; Antibodies, Neutralizing ; Antibodies, Viral ; Vaccines ; Protein Conformation
Chemical Substances	Viral Fusion Proteins ; Antibodies, Neutralizing ; Antibodies, Viral ; Vaccines
Language	English
Publishing date	2024-02-13
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/s41467-024-45480-z
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