Long-Read Sequencing Reveals Genetic Adaptation of Bartonella Adhesin A Among Different Bartonella henselae Isolates
(2022) In Frontiers in Microbiology 13.- Abstract
Bartonella henselae is the causative agent of cat scratch disease and other clinical entities such as endocarditis and bacillary angiomatosis. The life cycle of this pathogen, with alternating host conditions, drives evolutionary and host-specific adaptations. Human, feline, and laboratory adapted B. henselae isolates often display genomic and phenotypic differences that are related to the expression of outer membrane proteins, for example the Bartonella adhesin A (BadA). This modularly-structured trimeric autotransporter adhesin is a major virulence factor of B. henselae and is crucial for the initial binding to the host via the extracellular matrix proteins fibronectin and collagen. By using next-generation long-read sequencing we... (More)
Bartonella henselae is the causative agent of cat scratch disease and other clinical entities such as endocarditis and bacillary angiomatosis. The life cycle of this pathogen, with alternating host conditions, drives evolutionary and host-specific adaptations. Human, feline, and laboratory adapted B. henselae isolates often display genomic and phenotypic differences that are related to the expression of outer membrane proteins, for example the Bartonella adhesin A (BadA). This modularly-structured trimeric autotransporter adhesin is a major virulence factor of B. henselae and is crucial for the initial binding to the host via the extracellular matrix proteins fibronectin and collagen. By using next-generation long-read sequencing we demonstrate a conserved genome among eight B. henselae isolates and identify a variable genomic badA island with a diversified and highly repetitive badA gene flanked by badA pseudogenes. Two of the eight tested B. henselae strains lack BadA expression because of frameshift mutations. We suggest that active recombination mechanisms, possibly via phase variation (i.e., slipped-strand mispairing and site-specific recombination) within the repetitive badA island facilitate reshuffling of homologous domain arrays. The resulting variations among the different BadA proteins might contribute to host immune evasion and enhance long-term and efficient colonisation in the differing host environments. Considering the role of BadA as a key virulence factor, it remains important to check consistently and regularly for BadA surface expression during experimental infection procedures.
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- author
- Thibau, Arno ; Hipp, Katharina ; Vaca, Diana J ; Chowdhury, Sounak LU ; Malmström, Johan LU ; Saragliadis, Athanasios ; Ballhorn, Wibke ; Linke, Dirk and Kempf, Volkhard A J
- organization
- publishing date
- 2022
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Frontiers in Microbiology
- volume
- 13
- article number
- 838267
- publisher
- Frontiers Media S. A.
- external identifiers
-
- pmid:35197960
- scopus:85124938607
- ISSN
- 1664-302X
- DOI
- 10.3389/fmicb.2022.838267
- language
- English
- LU publication?
- yes
- id
- 285057dc-5309-4c92-a194-64af7a650b4c
- date added to LUP
- 2022-02-28 09:14:10
- date last changed
- 2024-04-18 06:01:48
@article{285057dc-5309-4c92-a194-64af7a650b4c, abstract = {{<p>Bartonella henselae is the causative agent of cat scratch disease and other clinical entities such as endocarditis and bacillary angiomatosis. The life cycle of this pathogen, with alternating host conditions, drives evolutionary and host-specific adaptations. Human, feline, and laboratory adapted B. henselae isolates often display genomic and phenotypic differences that are related to the expression of outer membrane proteins, for example the Bartonella adhesin A (BadA). This modularly-structured trimeric autotransporter adhesin is a major virulence factor of B. henselae and is crucial for the initial binding to the host via the extracellular matrix proteins fibronectin and collagen. By using next-generation long-read sequencing we demonstrate a conserved genome among eight B. henselae isolates and identify a variable genomic badA island with a diversified and highly repetitive badA gene flanked by badA pseudogenes. Two of the eight tested B. henselae strains lack BadA expression because of frameshift mutations. We suggest that active recombination mechanisms, possibly via phase variation (i.e., slipped-strand mispairing and site-specific recombination) within the repetitive badA island facilitate reshuffling of homologous domain arrays. The resulting variations among the different BadA proteins might contribute to host immune evasion and enhance long-term and efficient colonisation in the differing host environments. Considering the role of BadA as a key virulence factor, it remains important to check consistently and regularly for BadA surface expression during experimental infection procedures.</p>}}, author = {{Thibau, Arno and Hipp, Katharina and Vaca, Diana J and Chowdhury, Sounak and Malmström, Johan and Saragliadis, Athanasios and Ballhorn, Wibke and Linke, Dirk and Kempf, Volkhard A J}}, issn = {{1664-302X}}, language = {{eng}}, publisher = {{Frontiers Media S. A.}}, series = {{Frontiers in Microbiology}}, title = {{Long-Read Sequencing Reveals Genetic Adaptation of Bartonella Adhesin A Among Different Bartonella henselae Isolates}}, url = {{http://dx.doi.org/10.3389/fmicb.2022.838267}}, doi = {{10.3389/fmicb.2022.838267}}, volume = {{13}}, year = {{2022}}, }