Development of Anti- Yersinia pestis Human Antibodies with Features Required for Diagnostic and Therapeutic Applications

is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive...

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Published inImmunoTargets and therapy Vol. 9; pp. 299 - 316
Main Authors Lillo, Antonietta M, Velappan, Nileena, Kelliher, Julia M, Watts, Austin J, Merriman, Samuel P, Vuyisich, Grace, Lilley, Laura M, Coombs, Kent E, Mastren, Tara, Teshima, Munehiro, Stein, Benjamin W, Wagner, Gregory L, Iyer, Srinivas, Bradbury, Andrew R M, Harris, Jennifer Foster, Dichosa, Armand E, Kozimor, Stosh A
Format Journal Article
LanguageEnglish
Published New Zealand Dove Medical Press Limited 2020
Taylor & Francis Ltd
Dove Press
Dove
Dove Medical Press
Subjects
60 APPLIED LIFE SCIENCES
Agglutination
Antibiotics
Antibodies
Antigens
Bacteria
Cells (Biology)
Drug resistance
Enzyme-linked immunosorbent assay
Epithelial cells
Flow cytometry
Health aspects
immunoantibiotic
immunodiagnostic
Immunoglobulin G
Immunoreactivity
immunotherapy
lateral flow assay
LFA
Mammalian cells
Mass spectrometry
Mass spectroscopy
Microbial drug resistance
Monoclonal antibodies
Multidrug resistance
Mutation
National security
Original Research
Phages
Plague
Proteins
Public health
radioimmunotherapy
radiolabeling
RIT
Scientific equipment industry
Therapeutic applications
Therapeutics
Virulence
Yersinia pestis
United States
Massachusetts
United States > US
radioimmunotherapy
lateral flow assay
LFA
immunotherapy
immunodiagnostic
radiolabeling
RIT
immunoantibiotic
Online AccessGet full text

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Abstract is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness. Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays. Two of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding , and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected <1,000 cells in sandwich ELISA, did not harm respiratory epithelial cells, induced agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM). These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.
AbstractList BACKGROUNDYersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies Y. pestis as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive Y. pestis diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness.METHODSHere, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting Y. pestis fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays.RESULTSTwo of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding Y. pestis, and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected <1,000 Y. pestis cells in sandwich ELISA, did not harm respiratory epithelial cells, induced Y. pestis agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM).CONCLUSIONThese antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.
Antonietta M Lillo,1 Nileena Velappan,1 Julia M Kelliher,1 Austin J Watts,1 Samuel P Merriman,1 Grace Vuyisich,2 Laura M Lilley,2 Kent E Coombs,1 Tara Mastren,2 Munehiro Teshima,1 Benjamin W Stein,2 Gregory L Wagner,2 Srinivas Iyer,1 Andrew RM Bradbury,3 Jennifer Foster Harris,1 Armand E Dichosa,1 Stosh A Kozimor2 1Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM, USA; 2Chemistry Division, Los Alamos National Laboratory, Los Alamos, NM, USA; 3Specifica Inc., Santa Fe, NM, USACorrespondence: Antonietta M LilloUSA Department of Energy, In Care of Los Alamos National Laboratory, Bikini Atoll Road, SM-30, TA-43, Building 0001, Room 220, Los Alamos, NM 87545, USATel +1 505-606-0578Fax +1 505-665-9030Email alillo@lanl.govBackground: Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies Y. pestis as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive Y. pestis diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness.Methods: Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting Y. pestis fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays.Results: Two of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding Y. pestis, and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected < 1,000 Y. pestis cells in sandwich ELISA, did not harm respiratory epithelial cells, induced Y. pestis agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM).Conclusion: These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.Keywords: immunodiagnostic, radioimmunotherapy, RIT, immunotherapy, radiolabeling, immunoantibiotic, lateral flow assay, LFA
Background: Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies Y. pestis as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive Y. pestis diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness. Methods: Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting Y. pestis fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays. Results: Two of our anti-F1 IgG ([alpha]F1Ig 2 and [alpha]F1Ig8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding Y. pestis, and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected <1,000 Y. pestis cells in sandwich ELISA, did not harm respiratory epithelial cells, induced Y. pestis agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM). Conclusion: These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics. Keywords: immunodiagnostic, radioimmunotherapy, RIT, immunotherapy, radiolabeling, immunoantibiotic, lateral flow assay, LFA
Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies Y. pestis as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive Y. pestis diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness. Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting Y. pestis fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays. Two of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding Y. pestis, and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected < 1,000 Y. pestis cells in sandwich ELISA, did not harm respiratory epithelial cells, induced Y. pestis agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM). These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.
Background: Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies Y. pestis as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive Y. pestis diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness. Methods: Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting Y. pestis fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays. Results: Two of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding Y. pestis, and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected < 1,000 Y. pestis cells in sandwich ELISA, did not harm respiratory epithelial cells, induced Y. pestis agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM). Conclusion: These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.
is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance through natural or purposed means qualifies as a potential biothreat agent. Therefore, high-quality antibodies designed for accurate and sensitive diagnostics, and therapeutics potentiating or replacing traditional antibiotics are of utmost need for national security and public health preparedness. Here, we describe a set of human monoclonal immunoglobulins (IgG1s) targeting fraction 1 (F1) antigen, previously derived from in vitro evolution of a phage-display library of single-chain antibodies (scFv). We extensively characterized these antibodies and their effect on bacterial and mammalian cells via: ELISA, flow cytometry, mass spectrometry, spectroscopy, and various metabolic assays. Two of our anti-F1 IgG (αF1Ig 2 and αF1Ig 8) stood out for high production yield, specificity, and stability. These two antibodies were additionally attractive in that they displayed picomolar affinity, did not compete when binding , and retained immunoreactivity upon chemical derivatization. Most importantly, these antibodies detected <1,000 cells in sandwich ELISA, did not harm respiratory epithelial cells, induced agglutination at low concentration (350 nM), and caused apparent reduction in cell growth when radiolabeled at a nonagglutinating concentration (34 nM). These antibodies are amenable to the development of accurate and sensitive diagnostics and immuno/radioimmunotherapeutics.
Audience Academic
Author Coombs, Kent E
Harris, Jennifer Foster
Lilley, Laura M
Bradbury, Andrew R M
Kelliher, Julia M
Lillo, Antonietta M
Iyer, Srinivas
Velappan, Nileena
Wagner, Gregory L
Vuyisich, Grace
Mastren, Tara
Dichosa, Armand E
Kozimor, Stosh A
Watts, Austin J
Teshima, Munehiro
Merriman, Samuel P
Stein, Benjamin W
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CorporateAuthor Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
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Keywords radioimmunotherapy
lateral flow assay
LFA
immunotherapy
immunodiagnostic
radiolabeling
RIT
immunoantibiotic
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SSID ssj0000884122
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Snippet is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug resistance...
Background: Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or...
BACKGROUNDYersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or...
Yersinia pestis is a category A infective agent that causes bubonic, septicemic, and pneumonic plague. Notably, the acquisition of antimicrobial or multidrug...
Antonietta M Lillo,1 Nileena Velappan,1 Julia M Kelliher,1 Austin J Watts,1 Samuel P Merriman,1 Grace Vuyisich,2 Laura M Lilley,2 Kent E Coombs,1 Tara...
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StartPage 299
SubjectTerms 60 APPLIED LIFE SCIENCES
Agglutination
Antibiotics
Antibodies
Antigens
Bacteria
Cells (Biology)
Drug resistance
Enzyme-linked immunosorbent assay
Epithelial cells
Flow cytometry
Health aspects
immunoantibiotic
immunodiagnostic
Immunoglobulin G
Immunoreactivity
immunotherapy
lateral flow assay
LFA
Mammalian cells
Mass spectrometry
Mass spectroscopy
Microbial drug resistance
Monoclonal antibodies
Multidrug resistance
Mutation
National security
Original Research
Phages
Plague
Proteins
Public health
radioimmunotherapy
radiolabeling
RIT
Scientific equipment industry
Therapeutic applications
Therapeutics
Virulence
Yersinia pestis
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Title Development of Anti- Yersinia pestis Human Antibodies with Features Required for Diagnostic and Therapeutic Applications
URI https://www.ncbi.nlm.nih.gov/pubmed/33294421
https://www.proquest.com/docview/2470600872
https://search.proquest.com/docview/2468663268
https://www.osti.gov/servlets/purl/1755889
https://pubmed.ncbi.nlm.nih.gov/PMC7716875
https://doaj.org/article/d419f063afbd4c5c8e3e95e2976513b6
Volume 9
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