Stability Engineering of Recombinant Secretory IgA.

IgA aerosolization antibody engineering monoclonal antibody plant molecular pharming protein assembly protein stability secretory immunoglobulin A

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
22 Jun 2024
Historique:
received: 03 05 2024
revised: 19 06 2024
accepted: 19 06 2024
medline: 13 7 2024
pubmed: 13 7 2024
entrez: 13 7 2024
Statut: epublish

Résumé

Secretory IgA (SIgA) presents a promising avenue for mucosal immunotherapy yet faces challenges in expression, purification, and stability. IgA exists in two primary isotypes, IgA1 and IgA2, with IgA2 further subdivided into two common allotypes: IgA2m(1) and IgA2m(2). The major differences between IgA1 and IgA2 are located in the hinge region, with IgA1 featuring a 13-amino acid elongation that includes up to six

Identifiants

pubmed: 38999969
pii: ijms25136856
doi: 10.3390/ijms25136856
pii:
doi:

Substances chimiques

Immunoglobulin A, Secretory 0
Recombinant Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Austrian Science Fund
ID : J-4583
Organisme : BBSRC
ID : 21EBTA

Auteurs

Kathrin Göritzer (K)

Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Institute for Infection and Immunity, St. George's University of London, London SW17 0RE, UK.

Richard Strasser (R)

Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.

Julian K-C Ma (JK)

Institute for Infection and Immunity, St. George's University of London, London SW17 0RE, UK.

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Classifications MeSH