ArticleActa crystallographica. Section F, Structural biology communications2017
Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system from Porphyromonas gingivalis.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
- Deciphering the crystal structure of a novel nanobody against the NEIL1 DNA glycosylase.Acta crystallographica. Section D, Structural biology · 2024Article
- Fragment-based computational design of antibodies targeting structured epitopes.Science advances · 2022Article
- VInternational journal of molecular sciences · 2022Review
- Crystal structures of two camelid nanobodies raised against GldL, a component of the type IX secretion system from Flavobacterium johnsoniae.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Selection and Characterization of CSFV-Specific Single-Domain Antibodies and Their Application along with Immunomagnetic Nanobeads and Quantum Dots.BioMed research international · 2020Article
- Homology Modeling-Based in Silico Affinity Maturation Improves the Affinity of a Nanobody.International journal of molecular sciences · 2019Article
- Article
- Characterization and structure determination of a llama-derived nanobody targeting the J-base binding protein 1.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Type IX secretion system PorM and gliding machinery GldM form arches spanning the periplasmic space.Nature communications · 2018Article
- Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein.Microbial cell factories · 2017Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
PorM is a membrane protein that is involved in the assembly of the type IX secretion system (T9SS) in Porphyromonas gingivalis, a major bacterial pathogen that is responsible for periodontal disease in humans. In the context of structural studies of PorM to better understand T9SS assembly, four camelid nanobodies were selected, produced and purified, and their specific interaction with the N-terminal or C-terminal part of the periplasmic domain of PorM was investigated. Diffracting crystals were also obtained, and the structures of the four nanobodies were solved by molecular replacement. Furthermore, two nanobodies were used as crystallization chaperones and turned out to be valuable tools in the structure-determination process of the periplasmic domain of PorM.
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