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...
- 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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| 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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http://purl.org/coar/resource_type/c_2df8fbb1 |
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https://purl.org/redcol/resource_type/ART |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/article |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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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. |
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2165-0497 |
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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. |
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15 |
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5 |
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1 |
| dc.relation.citationvolume.spa.fl_str_mv |
10 |
| dc.relation.ispartofjournal.spa.fl_str_mv |
Microbiology Spectrum |
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15 páginas |
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American Society for Microbiology |
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Washington, Estados Unidos |
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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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