Highly Multiplexed Serology for Nonhuman Mammals

ABSTRACT: Emerging infectious diseases represent a serious and ongoing threat to humans. Most emerging viruses are maintained in stable relationships with other species of animals, and their emergence within the human population results from cross-species transmission. Therefore, if we want to be pr...

Full description

Autores:
López Quintero, Juan Álvaro
Piña, Alejandra
Metrailer, Morgan
Schuettenberg, Alexa
Peláez Sánchez, Ronald Guillermo
Agudelo Flórez, Piedad
Ryle, Luke
Monroy, Fernando
Altin, John
Tipo de recurso:
Article of investigation
Fecha de publicación:
2022
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/40503
Acceso en línea:
https://hdl.handle.net/10495/40503
Palabra clave:
Antibodies, Viral
Anticuerpos Antivirales
Antibody Formation
Formación de Anticuerpos
Enzyme-Linked Immunosorbent Assay
Ensayo de Inmunoadsorción Enzimática
Immunosorbents
Inmunoadsorbentes
Mammals
Mamíferos
https://id.nlm.nih.gov/mesh/D000914
https://id.nlm.nih.gov/mesh/D000917
https://id.nlm.nih.gov/mesh/D004797
https://id.nlm.nih.gov/mesh/D007164
https://id.nlm.nih.gov/mesh/D008322
Rights
openAccess
License
https://creativecommons.org/licenses/by/4.0/
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network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Highly Multiplexed Serology for Nonhuman Mammals
title Highly Multiplexed Serology for Nonhuman Mammals
spellingShingle Highly Multiplexed Serology for Nonhuman Mammals
Antibodies, Viral
Anticuerpos Antivirales
Antibody Formation
Formación de Anticuerpos
Enzyme-Linked Immunosorbent Assay
Ensayo de Inmunoadsorción Enzimática
Immunosorbents
Inmunoadsorbentes
Mammals
Mamíferos
https://id.nlm.nih.gov/mesh/D000914
https://id.nlm.nih.gov/mesh/D000917
https://id.nlm.nih.gov/mesh/D004797
https://id.nlm.nih.gov/mesh/D007164
https://id.nlm.nih.gov/mesh/D008322
title_short Highly Multiplexed Serology for Nonhuman Mammals
title_full Highly Multiplexed Serology for Nonhuman Mammals
title_fullStr Highly Multiplexed Serology for Nonhuman Mammals
title_full_unstemmed Highly Multiplexed Serology for Nonhuman Mammals
title_sort Highly Multiplexed Serology for Nonhuman Mammals
dc.creator.fl_str_mv López Quintero, Juan Álvaro
Piña, Alejandra
Metrailer, Morgan
Schuettenberg, Alexa
Peláez Sánchez, Ronald Guillermo
Agudelo Flórez, Piedad
Ryle, Luke
Monroy, Fernando
Altin, John
dc.contributor.author.none.fl_str_mv López Quintero, Juan Álvaro
Piña, Alejandra
Metrailer, Morgan
Schuettenberg, Alexa
Peláez Sánchez, Ronald Guillermo
Agudelo Flórez, Piedad
Ryle, Luke
Monroy, Fernando
Altin, John
dc.contributor.researchgroup.spa.fl_str_mv Inmunodeficiencias Primarias
dc.subject.decs.none.fl_str_mv Antibodies, Viral
Anticuerpos Antivirales
Antibody Formation
Formación de Anticuerpos
Enzyme-Linked Immunosorbent Assay
Ensayo de Inmunoadsorción Enzimática
Immunosorbents
Inmunoadsorbentes
Mammals
Mamíferos
topic Antibodies, Viral
Anticuerpos Antivirales
Antibody Formation
Formación de Anticuerpos
Enzyme-Linked Immunosorbent Assay
Ensayo de Inmunoadsorción Enzimática
Immunosorbents
Inmunoadsorbentes
Mammals
Mamíferos
https://id.nlm.nih.gov/mesh/D000914
https://id.nlm.nih.gov/mesh/D000917
https://id.nlm.nih.gov/mesh/D004797
https://id.nlm.nih.gov/mesh/D007164
https://id.nlm.nih.gov/mesh/D008322
dc.subject.meshuri.none.fl_str_mv https://id.nlm.nih.gov/mesh/D000914
https://id.nlm.nih.gov/mesh/D000917
https://id.nlm.nih.gov/mesh/D004797
https://id.nlm.nih.gov/mesh/D007164
https://id.nlm.nih.gov/mesh/D008322
description ABSTRACT: Emerging infectious diseases represent a serious and ongoing threat to humans. Most emerging viruses are maintained in stable relationships with other species of animals, and their emergence within the human population results from cross-species transmission. Therefore, if we want to be prepared for the next emerging virus, we need to broadly characterize the diversity and ecology of viruses currently infecting other animals (i.e., the animal virosphere). High-throughput metagenomic sequencing has accelerated the pace of virus discovery. However, molecular assays can detect only active infections and only if virus is present within the sampled fluid or tissue at the time of collection. In contrast, serological assays measure long-lived antibody responses to infections, which can be detected within the blood, regardless of the infected tissues. Therefore, serological assays can provide a complementary approach for understanding the circulation of viruses, and while serological assays have historically been limited in scope, recent advancements allow thousands to hundreds of thousands of antigens to be assessed simultaneously using <1 μL of blood (i.e., highly multiplexed serology). The application of highly multiplexed serology for the characterization of the animal virosphere is dependent on the availability of reagents that can be used to capture or label antibodies of interest. Here, we evaluate the utility of commercial immunoglobulin-binding proteins (protein A and protein G) to enable highly multiplexed serology in 25 species of nonhuman mammals, and we describe a competitive fluorescence-linked immunosorbent assay (FLISA) that can be used as an initial screen for choosing the most appropriate capture protein for a given host species. IMPORTANCE Antibodies are generated in response to infections with viruses and other pathogens, and they help protect against future exposures. Mature antibodies are long lived, are highly specific, and can bind to their protein targets with high affinity. Thus, antibodies can also provide information about an individual's history of viral exposures, which has important applications for understanding the epidemiology and etiology of disease. In recent years, there have been large advances in the available methods for broadly characterizing antibody-binding profiles, but thus far, these have been utilized primarily with human samples only. Here, we demonstrate that commercial antibody-binding reagents can facilitate modern antibody assays for a wide variety of mammalian species, and we describe an inexpensive and fast approach for choosing the best reagent for each animal species. By studying antibody-binding profiles in captive and wild animals, we can better understand the distribution and prevalence of viruses that could spill over into humans.
publishDate 2022
dc.date.issued.none.fl_str_mv 2022
dc.date.accessioned.none.fl_str_mv 2024-07-09T20:59:59Z
dc.date.available.none.fl_str_mv 2024-07-09T20:59:59Z
dc.type.spa.fl_str_mv Artículo de investigación
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dc.identifier.citation.spa.fl_str_mv Schuettenberg A, Piña A, Metrailer M, Peláez-Sánchez RG, Agudelo-Flórez P, Lopez JÁ, Ryle L, Monroy FP, Altin JA, Ladner JT. Highly Multiplexed Serology for Nonhuman Mammals. Microbiol Spectr. 2022 Oct 26;10(5):e0287322. doi: 10.1128/spectrum.02873-22.
dc.identifier.issn.none.fl_str_mv 2165-0497
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10495/40503
dc.identifier.doi.none.fl_str_mv 10.1128/spectrum.02873-22
identifier_str_mv Schuettenberg A, Piña A, Metrailer M, Peláez-Sánchez RG, Agudelo-Flórez P, Lopez JÁ, Ryle L, Monroy FP, Altin JA, Ladner JT. Highly Multiplexed Serology for Nonhuman Mammals. Microbiol Spectr. 2022 Oct 26;10(5):e0287322. doi: 10.1128/spectrum.02873-22.
2165-0497
10.1128/spectrum.02873-22
url https://hdl.handle.net/10495/40503
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Microbiol. Spectr.
dc.relation.citationendpage.spa.fl_str_mv 15
dc.relation.citationissue.spa.fl_str_mv 5
dc.relation.citationstartpage.spa.fl_str_mv 1
dc.relation.citationvolume.spa.fl_str_mv 10
dc.relation.ispartofjournal.spa.fl_str_mv Microbiology Spectrum
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dc.format.extent.spa.fl_str_mv 15 páginas
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dc.publisher.place.spa.fl_str_mv Washington, Estados Unidos
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spelling López Quintero, Juan ÁlvaroPiña, AlejandraMetrailer, MorganSchuettenberg, AlexaPeláez Sánchez, Ronald GuillermoAgudelo Flórez, PiedadRyle, LukeMonroy, FernandoAltin, JohnInmunodeficiencias Primarias2024-07-09T20:59:59Z2024-07-09T20:59:59Z2022Schuettenberg A, Piña A, Metrailer M, Peláez-Sánchez RG, Agudelo-Flórez P, Lopez JÁ, Ryle L, Monroy FP, Altin JA, Ladner JT. Highly Multiplexed Serology for Nonhuman Mammals. Microbiol Spectr. 2022 Oct 26;10(5):e0287322. doi: 10.1128/spectrum.02873-22.2165-0497https://hdl.handle.net/10495/4050310.1128/spectrum.02873-22ABSTRACT: Emerging infectious diseases represent a serious and ongoing threat to humans. Most emerging viruses are maintained in stable relationships with other species of animals, and their emergence within the human population results from cross-species transmission. Therefore, if we want to be prepared for the next emerging virus, we need to broadly characterize the diversity and ecology of viruses currently infecting other animals (i.e., the animal virosphere). High-throughput metagenomic sequencing has accelerated the pace of virus discovery. However, molecular assays can detect only active infections and only if virus is present within the sampled fluid or tissue at the time of collection. In contrast, serological assays measure long-lived antibody responses to infections, which can be detected within the blood, regardless of the infected tissues. Therefore, serological assays can provide a complementary approach for understanding the circulation of viruses, and while serological assays have historically been limited in scope, recent advancements allow thousands to hundreds of thousands of antigens to be assessed simultaneously using <1 μL of blood (i.e., highly multiplexed serology). The application of highly multiplexed serology for the characterization of the animal virosphere is dependent on the availability of reagents that can be used to capture or label antibodies of interest. Here, we evaluate the utility of commercial immunoglobulin-binding proteins (protein A and protein G) to enable highly multiplexed serology in 25 species of nonhuman mammals, and we describe a competitive fluorescence-linked immunosorbent assay (FLISA) that can be used as an initial screen for choosing the most appropriate capture protein for a given host species. IMPORTANCE Antibodies are generated in response to infections with viruses and other pathogens, and they help protect against future exposures. Mature antibodies are long lived, are highly specific, and can bind to their protein targets with high affinity. Thus, antibodies can also provide information about an individual's history of viral exposures, which has important applications for understanding the epidemiology and etiology of disease. In recent years, there have been large advances in the available methods for broadly characterizing antibody-binding profiles, but thus far, these have been utilized primarily with human samples only. Here, we demonstrate that commercial antibody-binding reagents can facilitate modern antibody assays for a wide variety of mammalian species, and we describe an inexpensive and fast approach for choosing the best reagent for each animal species. By studying antibody-binding profiles in captive and wild animals, we can better understand the distribution and prevalence of viruses that could spill over into humans.Colombia. Ministerio de Ciencia, Tecnología e InnovaciónNorthern Arizona UniversityCOL001242615 páginasapplication/pdfengAmerican Society for MicrobiologyWashington, Estados Unidoshttps://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/2.5/co/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Highly Multiplexed Serology for Nonhuman MammalsArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARThttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionAntibodies, ViralAnticuerpos AntiviralesAntibody FormationFormación de AnticuerposEnzyme-Linked Immunosorbent AssayEnsayo de Inmunoadsorción EnzimáticaImmunosorbentsInmunoadsorbentesMammalsMamíferoshttps://id.nlm.nih.gov/mesh/D000914https://id.nlm.nih.gov/mesh/D000917https://id.nlm.nih.gov/mesh/D004797https://id.nlm.nih.gov/mesh/D007164https://id.nlm.nih.gov/mesh/D008322Microbiol. 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