Affinity-Purification Combined with Crosslinking Mass Spectrometry for Identification and Structural Modeling of Host-Pathogen Protein-Protein Complexes
(2023) In Methods in molecular biology (Clifton, N.J.) p.181-200- Abstract
Host-pathogen protein-protein interactions are highly complex and dynamic and mediate key steps in pathogen adhesion to host, host invasion, and colonization as well as immune evasion. In bacteria, these interactions most often involve specialized virulence factors or effector proteins that specifically target central host proteins. Here, I present a mass spectrometry-based proteomics approach starting with the identification of host-pathogen interactions by affinity-purification followed by mapping the specific host-pathogen protein-protein interaction interfaces by crosslinking mass spectrometry and structural modeling of the complexes.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/977cdc12-82f5-41cd-bc35-058a48ea7938
- author
- Happonen, Lotta J. LU
- organization
- publishing date
- 2023
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Affinity-purification, Clusterin, Covalent crosslinking, Human blood plasma, Immunogenic secreted protein, Mass spectrometry, Protein, Protein interactions, Streptococcus pyogenes, Structural modeling, Virulence factor
- host publication
- Bacterial Pathogenesis : Book cover Book © 2023 Bacterial Pathogenesis Methods and Protocols - Book cover Book © 2023 Bacterial Pathogenesis Methods and Protocols
- series title
- Methods in molecular biology (Clifton, N.J.)
- editor
- Nordenfelt, Pontus and Collin, Mattias
- edition
- 2
- pages
- 181 - 200
- publisher
- Humana Press
- external identifiers
-
- pmid:37258968
- scopus:85160715282
- ISSN
- 1940-6029
- ISBN
- 978-1-0716-3242-0
- DOI
- 10.1007/978-1-0716-3243-7_12
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
- id
- 977cdc12-82f5-41cd-bc35-058a48ea7938
- date added to LUP
- 2023-06-12 22:02:03
- date last changed
- 2024-04-19 22:48:53
@inbook{977cdc12-82f5-41cd-bc35-058a48ea7938, abstract = {{<p>Host-pathogen protein-protein interactions are highly complex and dynamic and mediate key steps in pathogen adhesion to host, host invasion, and colonization as well as immune evasion. In bacteria, these interactions most often involve specialized virulence factors or effector proteins that specifically target central host proteins. Here, I present a mass spectrometry-based proteomics approach starting with the identification of host-pathogen interactions by affinity-purification followed by mapping the specific host-pathogen protein-protein interaction interfaces by crosslinking mass spectrometry and structural modeling of the complexes.</p>}}, author = {{Happonen, Lotta J.}}, booktitle = {{Bacterial Pathogenesis : Book cover Book © 2023 Bacterial Pathogenesis Methods and Protocols}}, editor = {{Nordenfelt, Pontus and Collin, Mattias}}, isbn = {{978-1-0716-3242-0}}, issn = {{1940-6029}}, keywords = {{Affinity-purification; Clusterin; Covalent crosslinking; Human blood plasma; Immunogenic secreted protein; Mass spectrometry; Protein; Protein interactions; Streptococcus pyogenes; Structural modeling; Virulence factor}}, language = {{eng}}, pages = {{181--200}}, publisher = {{Humana Press}}, series = {{Methods in molecular biology (Clifton, N.J.)}}, title = {{Affinity-Purification Combined with Crosslinking Mass Spectrometry for Identification and Structural Modeling of Host-Pathogen Protein-Protein Complexes}}, url = {{http://dx.doi.org/10.1007/978-1-0716-3243-7_12}}, doi = {{10.1007/978-1-0716-3243-7_12}}, year = {{2023}}, }