A new C-type lectin similar to the human immunoreceptor DC-SIGN mediates symbiont acquisition by a marine nematode.
Appl Environ Microbiol
; 72(4): 2950-6, 2006 Apr.
Article
en En
| MEDLINE
| ID: mdl-16598002
Although thiotrophic symbioses have been intensively studied for the last three decades, nothing is known about the molecular mechanisms of symbiont acquisition. We used the symbiosis between the marine nematode Laxus oneistus and sulfur-oxidizing bacteria to study this process. In this association a monolayer of symbionts covers the whole cuticle of the nematode, except its anterior-most region. Here, we identify a novel Ca(2+)-dependent mannose-specific lectin that was exclusively secreted onto the posterior, bacterium-associated region of L. oneistus cuticle. A recombinant form of this lectin induced symbiont aggregation in seawater and was able to compete with the native lectin for symbiont binding in vivo. Surprisingly, the carbohydrate recognition domain of this mannose-binding protein was similar both structurally and functionally to a human dendritic cell-specific immunoreceptor. Our results provide a molecular link between bacterial symbionts and host-secreted mucus in a marine symbiosis and suggest conservation in the mechanisms of host-microbe interactions throughout the animal kingdom.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Agua de Mar
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Simbiosis
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Bacterias
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Moléculas de Adhesión Celular
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Receptores de Superficie Celular
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Lectinas Tipo C
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Lectinas de Unión a Manosa
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Nematodos
Tipo de estudio:
Prognostic_studies
Límite:
Animals
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Humans
Idioma:
En
Revista:
Appl Environ Microbiol
Año:
2006
Tipo del documento:
Article
País de afiliación:
Austria