Single domain antibodies: promising experimental and therapeutic tools in infection and immunity
- Autores
- Wesolowski, Janusz; Alzogaray, Vanina Andrea; Reyelt, Jan; Unger, Mandy; Juarez, Karla; Urrutia, Mariela; Cauerhff, Ana Albina; Danquah, Welbeck; Rissiek, Björn; Scheuplein, Felix; Schwarz, Nicole; Adriouch, Sahil; Boyer, Olivier; Seman, Michel; Licea, Alexei; Serreze, David V.; Goldbaum, Fernando Alberto; Haag, Friedrich; Koch Nolte, Friedrich
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes.
Centro de Investigación y Desarrollo en Fermentaciones Industriales - Materia
-
Biología
Enzyme inhibitors
Nanobody
Recombinant antibodies
Single domain antibodies
VHH
Virus neutralization - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
.jpg)
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/104354
Ver los metadatos del registro completo
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Single domain antibodies: promising experimental and therapeutic tools in infection and immunityWesolowski, JanuszAlzogaray, Vanina AndreaReyelt, JanUnger, MandyJuarez, KarlaUrrutia, MarielaCauerhff, Ana AlbinaDanquah, WelbeckRissiek, BjörnScheuplein, FelixSchwarz, NicoleAdriouch, SahilBoyer, OlivierSeman, MichelLicea, AlexeiSerreze, David V.Goldbaum, Fernando AlbertoHaag, FriedrichKoch Nolte, FriedrichBiologíaEnzyme inhibitorsNanobodyRecombinant antibodiesSingle domain antibodiesVHHVirus neutralizationAntibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes.Centro de Investigación y Desarrollo en Fermentaciones Industriales2009-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf157-174http://sedici.unlp.edu.ar/handle/10915/104354enginfo:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/36849info:eu-repo/semantics/altIdentifier/issn/0300-8584info:eu-repo/semantics/altIdentifier/doi/10.1007/s00430-009-0116-7info:eu-repo/semantics/altIdentifier/hdl/11336/36849info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:54:55Zoai:sedici.unlp.edu.ar:10915/104354Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:54:56.168SEDICI (UNLP) - Universidad Nacional de La Platafalse |
| dc.title.none.fl_str_mv |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| title |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| spellingShingle |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity Wesolowski, Janusz Biología Enzyme inhibitors Nanobody Recombinant antibodies Single domain antibodies VHH Virus neutralization |
| title_short |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| title_full |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| title_fullStr |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| title_full_unstemmed |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| title_sort |
Single domain antibodies: promising experimental and therapeutic tools in infection and immunity |
| dc.creator.none.fl_str_mv |
Wesolowski, Janusz Alzogaray, Vanina Andrea Reyelt, Jan Unger, Mandy Juarez, Karla Urrutia, Mariela Cauerhff, Ana Albina Danquah, Welbeck Rissiek, Björn Scheuplein, Felix Schwarz, Nicole Adriouch, Sahil Boyer, Olivier Seman, Michel Licea, Alexei Serreze, David V. Goldbaum, Fernando Alberto Haag, Friedrich Koch Nolte, Friedrich |
| author |
Wesolowski, Janusz |
| author_facet |
Wesolowski, Janusz Alzogaray, Vanina Andrea Reyelt, Jan Unger, Mandy Juarez, Karla Urrutia, Mariela Cauerhff, Ana Albina Danquah, Welbeck Rissiek, Björn Scheuplein, Felix Schwarz, Nicole Adriouch, Sahil Boyer, Olivier Seman, Michel Licea, Alexei Serreze, David V. Goldbaum, Fernando Alberto Haag, Friedrich Koch Nolte, Friedrich |
| author_role |
author |
| author2 |
Alzogaray, Vanina Andrea Reyelt, Jan Unger, Mandy Juarez, Karla Urrutia, Mariela Cauerhff, Ana Albina Danquah, Welbeck Rissiek, Björn Scheuplein, Felix Schwarz, Nicole Adriouch, Sahil Boyer, Olivier Seman, Michel Licea, Alexei Serreze, David V. Goldbaum, Fernando Alberto Haag, Friedrich Koch Nolte, Friedrich |
| author2_role |
author author author author author author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Biología Enzyme inhibitors Nanobody Recombinant antibodies Single domain antibodies VHH Virus neutralization |
| topic |
Biología Enzyme inhibitors Nanobody Recombinant antibodies Single domain antibodies VHH Virus neutralization |
| dc.description.none.fl_txt_mv |
Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes. Centro de Investigación y Desarrollo en Fermentaciones Industriales |
| description |
Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes. |
| publishDate |
2009 |
| dc.date.none.fl_str_mv |
2009-08 |
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eng |
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eng |
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