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Article ; Online: Nucleocapsid protein-specific monoclonal antibodies protect mice against Crimean-Congo hemorrhagic fever virus.

Garrison, Aura R / Moresco, Vanessa / Zeng, Xiankun / Cline, Curtis R / Ward, Michael D / Ricks, Keersten M / Olschner, Scott P / Cazares, Lisa H / Karaaslan, Elif / Fitzpatrick, Collin J / Bergeron, Éric / Pegan, Scott D / Golden, Joseph W

Nature communications

2024 Volume 15, Issue 1, Page(s) 1722

Abstract: Crimean-Congo hemorrhagic fever virus (CCHFV) is a WHO priority pathogen. Antibody-based medical countermeasures offer an important strategy to mitigate severe disease caused by CCHFV. Most efforts have focused on targeting the viral glycoproteins. ... ...

Abstract	Crimean-Congo hemorrhagic fever virus (CCHFV) is a WHO priority pathogen. Antibody-based medical countermeasures offer an important strategy to mitigate severe disease caused by CCHFV. Most efforts have focused on targeting the viral glycoproteins. However, glycoproteins are poorly conserved among viral strains. The CCHFV nucleocapsid protein (NP) is highly conserved between CCHFV strains. Here, we investigate the protective efficacy of a CCHFV monoclonal antibody targeting the NP. We find that an anti-NP monoclonal antibody (mAb-9D5) protected female mice against lethal CCHFV infection or resulted in a significant delay in mean time-to-death in mice that succumbed to disease compared to isotype control animals. Antibody protection is independent of Fc-receptor functionality and complement activity. The antibody bound NP from several CCHFV strains and exhibited robust cross-protection against the heterologous CCHFV strain Afg09-2990. Our work demonstrates that the NP is a viable target for antibody-based therapeutics, providing another direction for developing immunotherapeutics against CCHFV.
MeSH term(s)	Female ; Animals ; Mice ; Hemorrhagic Fever Virus, Crimean-Congo/metabolism ; Nucleocapsid Proteins/metabolism ; Antibodies, Monoclonal ; Hemorrhagic Fever, Crimean/prevention & control ; Glycoproteins/metabolism ; Antibodies, Viral
Chemical Substances	Nucleocapsid Proteins ; Antibodies, Monoclonal ; Glycoproteins ; Antibodies, Viral
Language	English
Publishing date	2024-02-26
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/s41467-024-46110-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Species-specific quantification of circulating ebolavirus burden using VP40-derived peptide variants.

Shu, Qingbo / Kenny, Tara / Fan, Jia / Lyon, Christopher J / Cazares, Lisa H / Hu, Tony Y

PLoS pathogens

2021 Volume 17, Issue 11, Page(s) e1010039

Abstract: Six ebolavirus species are reported to date, including human pathogens Bundibugyo virus (BDBV), Ebola virus (EBOV), Sudan virus (SUDV), and Taï Forest virus (TAFV); non-human pathogen Reston virus (RESTV); and the plausible Bombali virus (BOMV). Since ... ...

Abstract	Six ebolavirus species are reported to date, including human pathogens Bundibugyo virus (BDBV), Ebola virus (EBOV), Sudan virus (SUDV), and Taï Forest virus (TAFV); non-human pathogen Reston virus (RESTV); and the plausible Bombali virus (BOMV). Since there are differences in the disease severity caused by different species, species identification and viral burden quantification are critical for treating infected patients timely and effectively. Here we developed an immunoprecipitation-coupled mass spectrometry (IP-MS) assay for VP40 antigen detection and quantification. We carefully selected two regions of VP40, designated as peptide 8 and peptide12 from the protein sequence that showed minor variations among Ebolavirus species through MS analysis of tryptic peptides and antigenicity prediction based on available bioinformatic tools, and generated high-quality capture antibodies pan-specific for these variant peptides. We applied this assay to human plasma spiked with recombinant VP40 protein from EBOV, SUDV, and BDBV and virus-like particles (VLP), as well as EBOV infected NHP plasma. Sequence substitutions between EBOV and SUDV, the two species with highest lethality, produced affinity variations of 2.6-fold for p8 and 19-fold for p12. The proposed IP-MS assay differentiates four of the six known EBV species in one assay, through a combination of p8 and p12 data. The IP-MS assay limit of detection (LOD) using multiple reaction monitoring (MRM) as signal readout was determined to be 28 ng/mL and 7 ng/mL for EBOV and SUDV respectively, equivalent to ~1.625-6.5×105 Geq/mL, and comparable to the LOD of lateral flow immunoassays currently used for Ebola surveillance. The two peptides of the IP-MS assay were also identified by their tandem MS spectra using a miniature MALDI-TOF MS instrument, greatly increasing the feasibility of high specificity assay in a decentralized laboratory.
MeSH term(s)	Animals ; Ebolavirus/immunology ; Hemorrhagic Fever, Ebola/blood ; Hemorrhagic Fever, Ebola/diagnosis ; Hemorrhagic Fever, Ebola/immunology ; Hemorrhagic Fever, Ebola/virology ; Humans ; Macaca mulatta ; Peptide Fragments/immunology ; Recombinant Proteins/immunology ; Species Specificity ; Viral Matrix Proteins/immunology
Chemical Substances	Peptide Fragments ; Recombinant Proteins ; VP40 protein, virus ; Viral Matrix Proteins
Language	English
Publishing date	2021-11-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1010039
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Article ; Online: Metabolomic Profiling of Human Urine Samples Using LC-TIMS-QTOF Mass Spectrometry.

Di Poto, Cristina / Tian, Xiang / Peng, Xuejun / Heyman, Heino M / Szesny, Matthias / Hess, Sonja / Cazares, Lisa H

Journal of the American Society for Mass Spectrometry

2021 Volume 32, Issue 8, Page(s) 2072–2080

Abstract: The identification of metabolites in biological samples is challenging due to their chemical and structural diversity. Ion mobility spectrometry (IMS) separates ionized molecules based on their mobility in a carrier buffer gas giving information about ... ...

Abstract	The identification of metabolites in biological samples is challenging due to their chemical and structural diversity. Ion mobility spectrometry (IMS) separates ionized molecules based on their mobility in a carrier buffer gas giving information about the ionic shape by measuring the rotationally averaged collision cross-section (CCS) value. This orthogonal descriptor, in combination with the
MeSH term(s)	Chromatography, Reverse-Phase ; Healthy Volunteers ; Humans ; Ion Mobility Spectrometry/methods ; Mass Spectrometry/methods ; Metabolomics/methods ; Phenylalanine/urine ; Reproducibility of Results ; Tryptophan/urine ; Tyrosine/urine ; Urinalysis/methods ; Urine/chemistry
Chemical Substances	Tyrosine (42HK56048U) ; Phenylalanine (47E5O17Y3R) ; Tryptophan (8DUH1N11BX)
Language	English
Publishing date	2021-06-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	1073671-2
ISSN	1879-1123 ; 1044-0305
ISSN (online)	1879-1123
ISSN	1044-0305
DOI	10.1021/jasms.0c00467
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Article: Paracrine IFN Response Limits ZIKV Infection in Human Sertoli Cells.

Strange, Daniel P / Jiyarom, Boonyanudh / Sadri-Ardekani, Hooman / Cazares, Lisa H / Kenny, Tara A / Ward, Michael D / Verma, Saguna

Frontiers in microbiology

2021 Volume 12, Page(s) 667146

Abstract: Zika virus (ZIKV) is unique among mosquito-borne flaviviruses in its ability to be sexually transmitted. The testes have been implicated as sites of long-term ZIKV replication, and our previous studies have identified Sertoli cells (SC), the nurse cells ... ...

Abstract	Zika virus (ZIKV) is unique among mosquito-borne flaviviruses in its ability to be sexually transmitted. The testes have been implicated as sites of long-term ZIKV replication, and our previous studies have identified Sertoli cells (SC), the nurse cells of the seminiferous epithelium that govern spermatogenesis, as major targets of ZIKV infection. To improve our understanding of the interaction of ZIKV with human SC, we analyzed ZIKV-induced proteome changes in these cells using high-throughput liquid chromatography-tandem mass spectrometry (LC-MS/MS). Our data demonstrated that interferon (IFN) signaling was the most significantly enriched pathway and the antiviral proteins MX1 and IFIT1 were among the top upregulated proteins in SC following ZIKV infection. The dynamic between IFN response and ZIKV infection kinetics in SC remains unclear, therefore we further determined whether MX1 and IFIT1 serve as antiviral effectors against ZIKV. We found that increased levels of MX1 at the later time points of infection coincided with diminished ZIKV infection while the silencing of
Language	English
Publishing date	2021-05-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.667146
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Article ; Online: CCL5-CCR5 interactions modulate metabolic events during tumor onset to promote tumorigenesis.

Gao, Darrin / Cazares, Lisa H / Fish, Eleanor N

BMC cancer

2017 Volume 17, Issue 1, Page(s) 834

Abstract: Background: In earlier studies we have shown that CCL5 activation of CCR5 induces the proliferation and survival of breast cancer cells in a mechanistic target of rapamycin (mTOR)-dependent manner and that this is in part due to CCR5-mediated increases ... ...

Abstract	Background: In earlier studies we have shown that CCL5 activation of CCR5 induces the proliferation and survival of breast cancer cells in a mechanistic target of rapamycin (mTOR)-dependent manner and that this is in part due to CCR5-mediated increases in glycolytic metabolism. Methods: Using the MDA-MB-231 triple negative human breast cancer cell line and mouse mammary tumor virus - polyomavirus middle T-antigen (MMTV-PyMT) mouse primary breast cancer cells, we conducted in vivo tumor transplant experiments to examine the effects of CCL5-CCR5 interactions in the context of regulating tumor metabolism. Additionally, we employed Matrix-Assisted Laser Desorption/Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry imaging (MALDI-FTICR-MSI) to evaluate tumor utilization of cellular metabolites. Results: We provide evidence that, in the absence of CCR5, the early events associated with rapid tumor growth in the MMTV-PyMT mouse model of spontaneous breast cancer development, are diminished, as demonstrated by a delay in tumor onset. In tumor transplant studies into immunocompromised mice we identify a direct correlation between reduced tumor proliferation and decreased metabolic activity, specifically associated with tumor expression of CCR5. The reduction in tumorigenesis is accompanied by decreases in glucose uptake, glucose transporter-1 (GLUT-1) cell surface expression, intracellular ATP and lactate levels, as well as reduced CCL5 production. Using MALDI-FTICR-MS, we show that the rapid early tumor growth of CCR5 Conclusions: These findings suggest that CCL5-CCR5 interactions in the tumor microenvironment modulate metabolic events during tumor onset to promote tumorigenesis.
MeSH term(s)	Animals ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Carcinogenesis/metabolism ; Cell Line, Tumor ; Chemokine CCL5/metabolism ; Female ; Glycolysis ; Humans ; Mice ; Mice, Inbred NOD ; Receptors, CCR5/metabolism ; Tumor Cells, Cultured
Chemical Substances	Chemokine CCL5 ; Receptors, CCR5
Language	English
Publishing date	2017--08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1471-2407
ISSN (online)	1471-2407
DOI	10.1186/s12885-017-3817-0
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Article ; Online: Thermal inactivation of enzymes and pathogens in biosamples for MS analysis.

Ahnoff, Martin / Cazares, Lisa H / Sköld, Karl

Bioanalysis

2015 Volume 7, Issue 15, Page(s) 1885–1899

Abstract: Protein denaturation is the common basis for enzyme inactivation and inactivation of pathogens, necessary for preservation and safe handling of biosamples for downstream analysis. While heat-stabilization technology has been used in proteomic and ... ...

Abstract	Protein denaturation is the common basis for enzyme inactivation and inactivation of pathogens, necessary for preservation and safe handling of biosamples for downstream analysis. While heat-stabilization technology has been used in proteomic and peptidomic research since its introduction in 2009, the advantages of using the technique for simultaneous pathogen inactivation have only recently been addressed. The time required for enzyme inactivation by heat (≈1 min) is short compared with chemical treatments, and inactivation is irreversible in contrast to freezing. Heat stabilization thus facilitates mass spectrometric studies of biomolecules with a fast conversion rate, and expands the chemical space of potential biomarkers to include more short-lived entities, such as phosphorylated proteins, in tissue samples as well as whole-blood (dried blood sample) samples.
MeSH term(s)	Mass Spectrometry/methods ; Protein Denaturation ; Proteomics/methods ; Tissue Fixation
Language	English
Publishing date	2015
Publishing country	England
Document type	Journal Article
ISSN	1757-6199
ISSN (online)	1757-6199
DOI	10.4155/bio.15.122
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Article ; Online: Species-specific quantification of circulating ebolavirus burden using VP40-derived peptide variants.

Qingbo Shu / Tara Kenny / Jia Fan / Christopher J Lyon / Lisa H Cazares / Tony Y Hu

PLoS Pathogens, Vol 17, Iss 11, p e

2021 Volume 1010039

Abstract	Six ebolavirus species are reported to date, including human pathogens Bundibugyo virus (BDBV), Ebola virus (EBOV), Sudan virus (SUDV), and Taï Forest virus (TAFV); non-human pathogen Reston virus (RESTV); and the plausible Bombali virus (BOMV). Since there are differences in the disease severity caused by different species, species identification and viral burden quantification are critical for treating infected patients timely and effectively. Here we developed an immunoprecipitation-coupled mass spectrometry (IP-MS) assay for VP40 antigen detection and quantification. We carefully selected two regions of VP40, designated as peptide 8 and peptide12 from the protein sequence that showed minor variations among Ebolavirus species through MS analysis of tryptic peptides and antigenicity prediction based on available bioinformatic tools, and generated high-quality capture antibodies pan-specific for these variant peptides. We applied this assay to human plasma spiked with recombinant VP40 protein from EBOV, SUDV, and BDBV and virus-like particles (VLP), as well as EBOV infected NHP plasma. Sequence substitutions between EBOV and SUDV, the two species with highest lethality, produced affinity variations of 2.6-fold for p8 and 19-fold for p12. The proposed IP-MS assay differentiates four of the six known EBV species in one assay, through a combination of p8 and p12 data. The IP-MS assay limit of detection (LOD) using multiple reaction monitoring (MRM) as signal readout was determined to be 28 ng/mL and 7 ng/mL for EBOV and SUDV respectively, equivalent to ~1.625-6.5×105 Geq/mL, and comparable to the LOD of lateral flow immunoassays currently used for Ebola surveillance. The two peptides of the IP-MS assay were also identified by their tandem MS spectra using a miniature MALDI-TOF MS instrument, greatly increasing the feasibility of high specificity assay in a decentralized laboratory.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Species-specific quantification of circulating ebolavirus burden using VP40-derived peptide variants

Qingbo Shu / Tara Kenny / Jia Fan / Christopher J. Lyon / Lisa H. Cazares / Tony Y. Hu

PLoS Pathogens, Vol 17, Iss

2021 Volume 11

Abstract	Six ebolavirus species are reported to date, including human pathogens Bundibugyo virus (BDBV), Ebola virus (EBOV), Sudan virus (SUDV), and Taï Forest virus (TAFV); non-human pathogen Reston virus (RESTV); and the plausible Bombali virus (BOMV). Since there are differences in the disease severity caused by different species, species identification and viral burden quantification are critical for treating infected patients timely and effectively. Here we developed an immunoprecipitation-coupled mass spectrometry (IP-MS) assay for VP40 antigen detection and quantification. We carefully selected two regions of VP40, designated as peptide 8 and peptide12 from the protein sequence that showed minor variations among Ebolavirus species through MS analysis of tryptic peptides and antigenicity prediction based on available bioinformatic tools, and generated high-quality capture antibodies pan-specific for these variant peptides. We applied this assay to human plasma spiked with recombinant VP40 protein from EBOV, SUDV, and BDBV and virus-like particles (VLP), as well as EBOV infected NHP plasma. Sequence substitutions between EBOV and SUDV, the two species with highest lethality, produced affinity variations of 2.6-fold for p8 and 19-fold for p12. The proposed IP-MS assay differentiates four of the six known EBV species in one assay, through a combination of p8 and p12 data. The IP-MS assay limit of detection (LOD) using multiple reaction monitoring (MRM) as signal readout was determined to be 28 ng/mL and 7 ng/mL for EBOV and SUDV respectively, equivalent to ~1.625–6.5×105 Geq/mL, and comparable to the LOD of lateral flow immunoassays currently used for Ebola surveillance. The two peptides of the IP-MS assay were also identified by their tandem MS spectra using a miniature MALDI-TOF MS instrument, greatly increasing the feasibility of high specificity assay in a decentralized laboratory. Author summary We developed a quantitative assay for carefully selected species-specific VP40 peptide variants by selecting two VP40 ...
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	540
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Proteomic Analysis of Non-human Primate Peripheral Blood Mononuclear Cells During

Chiang, Chih-Yuan / Zhong, Yang / Ward, Michael D / Lane, Douglas J / Kenny, Tara / Rosario-Acevedo, Raysa / Eaton, Brett P / Treviño, Sylvia R / Chance, Taylor B / Hu, Meghan / Worsham, Patricia L / Waag, David M / Moore, Richard T / Cazares, Lisa H / Cote, Christopher K / Zhou, Yingyao / Panchal, Rekha G

Frontiers in microbiology

2021 Volume 12, Page(s) 625211

Abstract: Burkholderia ... ...

Abstract	Burkholderia mallei
Language	English
Publishing date	2021-04-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.625211
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Article ; Online: Characterization of Citrullination Sites in Neutrophils and Mast Cells Activated by Ionomycin via Integration of Mass Spectrometry and Machine Learning.

Chaerkady, Raghothama / Zhou, Yebin / Delmar, Jared A / Weng, Shao Huan Samuel / Wang, Junmin / Awasthi, Shivangi / Sims, Dorothy / Bowen, Michael A / Yu, Wen / Cazares, Lisa H / Sims, Gary P / Hess, Sonja

Journal of proteome research

2021 Volume 20, Issue 6, Page(s) 3150–3164

Abstract: Citrullination is an important post-translational modification implicated in many diseases including rheumatoid arthritis (RA), Alzheimer's disease, and cancer. Neutrophil and mast cells have different expression profiles for protein-arginine deiminases ( ...

Abstract	Citrullination is an important post-translational modification implicated in many diseases including rheumatoid arthritis (RA), Alzheimer's disease, and cancer. Neutrophil and mast cells have different expression profiles for protein-arginine deiminases (PADs), and ionomycin-induced activation makes them an ideal cellular model to study proteins susceptible to citrullination. We performed high-resolution mass spectrometry and stringent data filtration to identify citrullination sites in neutrophil and mast cells treated with and without ionomycin. We identified a total of 833 validated citrullination sites on 395 proteins. Several of these citrullinated proteins are important components of pathways involved in innate immune responses. Using this benchmark primary sequence data set, we developed machine learning models to predict citrullination in neutrophil and mast cell proteins. We show that our models predict citrullination likelihood with 0.735 and 0.766 AUCs (area under the receiver operating characteristic curves), respectively, on independent validation sets. In summary, this study provides the largest number of validated citrullination sites in neutrophil and mast cell proteins. The use of our novel motif analysis approach to predict citrullination sites will facilitate the discovery of novel protein substrates of protein-arginine deiminases (PADs), which may be key to understanding immunopathologies of various diseases.
MeSH term(s)	Citrullination ; Citrulline/metabolism ; Ionomycin/pharmacology ; Machine Learning ; Mass Spectrometry ; Mast Cells/metabolism ; Neutrophils/metabolism ; Protein-Arginine Deiminases/genetics
Chemical Substances	Citrulline (29VT07BGDA) ; Ionomycin (56092-81-0) ; Protein-Arginine Deiminases (EC 3.5.3.15)
Language	English
Publishing date	2021-05-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.1c00028
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ab Jg. 2022: Lesesaal (EG)

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