IRIS publication 241507050
Influence of internalin A murinisation on host resistance to orally acquired listeriosis in mice.
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TY - JOUR - Bergmann S, Beard PM, Pasche B, Lienenklaus S, Weiss S, Gahan CG, Schughart K, Lengeling A - 2013 - April - BMC Microbiology - Influence of internalin A murinisation on host resistance to orally acquired listeriosis in mice. - Validated - () - 13 - The bacterial surface protein internalin (InlA) is a major virulence factor of the food-born pathogen Listeria monocytogenes. It plays a critical role in the bacteria crossing the host intestinal barrier by a species-specific interaction with the cell adhesion molecule E-cadherin. In mice, the interaction of InlA with murine E-cadherin is impaired due to sequence-specific binding incompatibilities. We have previously used the approach of 'murinisation' to establish an oral listeriosis infection model in mice by exchanging two amino acid residues in InlA. This dramatically increases binding to mouse E-cadherin. In the present study, we have used bioluminescent murinised and non-murinised Listeria strains to examine the spatiotemporal dissemination of Listeria in four diverse mouse genetic backgrounds after oral inoculation. - 10.1186/1471-2180-13-90 DA - 2013/04 ER -
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@article{V241507050, = {Bergmann S, Beard PM and Pasche B, Lienenklaus S and Weiss S, Gahan CG and Schughart K, Lengeling A }, = {2013}, = {April}, = {BMC Microbiology}, = {Influence of internalin A murinisation on host resistance to orally acquired listeriosis in mice.}, = {Validated}, = {()}, = {13}, = {{The bacterial surface protein internalin (InlA) is a major virulence factor of the food-born pathogen Listeria monocytogenes. It plays a critical role in the bacteria crossing the host intestinal barrier by a species-specific interaction with the cell adhesion molecule E-cadherin. In mice, the interaction of InlA with murine E-cadherin is impaired due to sequence-specific binding incompatibilities. We have previously used the approach of 'murinisation' to establish an oral listeriosis infection model in mice by exchanging two amino acid residues in InlA. This dramatically increases binding to mouse E-cadherin. In the present study, we have used bioluminescent murinised and non-murinised Listeria strains to examine the spatiotemporal dissemination of Listeria in four diverse mouse genetic backgrounds after oral inoculation.}}, = {10.1186/1471-2180-13-90}, source = {IRIS} }
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AUTHORS | Bergmann S, Beard PM, Pasche B, Lienenklaus S, Weiss S, Gahan CG, Schughart K, Lengeling A | ||
YEAR | 2013 | ||
MONTH | April | ||
JOURNAL_CODE | BMC Microbiology | ||
TITLE | Influence of internalin A murinisation on host resistance to orally acquired listeriosis in mice. | ||
STATUS | Validated | ||
TIMES_CITED | () | ||
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VOLUME | 13 | ||
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ABSTRACT | The bacterial surface protein internalin (InlA) is a major virulence factor of the food-born pathogen Listeria monocytogenes. It plays a critical role in the bacteria crossing the host intestinal barrier by a species-specific interaction with the cell adhesion molecule E-cadherin. In mice, the interaction of InlA with murine E-cadherin is impaired due to sequence-specific binding incompatibilities. We have previously used the approach of 'murinisation' to establish an oral listeriosis infection model in mice by exchanging two amino acid residues in InlA. This dramatically increases binding to mouse E-cadherin. In the present study, we have used bioluminescent murinised and non-murinised Listeria strains to examine the spatiotemporal dissemination of Listeria in four diverse mouse genetic backgrounds after oral inoculation. | ||
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DOI_LINK | 10.1186/1471-2180-13-90 | ||
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