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Affinity-Purification Combined with Crosslinking Mass Spectrometry for Identification and Structural Modeling of Host-Pathogen Protein-Protein Complexes

Happonen, Lotta J. LU (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:
author
organization
publishing date
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}},
}