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The gill symbiont of the hydrothermal vent mussel Bathymodiolus thermophilus is a psychrophilic,chemoautotrophic, sulfur bacterium
Authors:D C Nelson  K D Hagen  D B Edwards
Institution:(1) Section of Microbiology, University of California at Davis, Hutchison Hall, 95616 Davis, California, USA;(2) Marine Biology Research Division, Scripps Institution of Oceanography, University of California at San Diego, 92093-0202 LA Jolla, California, USA
Abstract:Certain hydrothermal vent invertebrates, e.g. Riftia pachyptila and Calyptogena magnifica, are clearly established as harboring dense populations of chemoautotrophic sulfur bacteria in specialized tissues. By contrast, the physiological characteristics of the abundant intracellular gill symbiont of the vent mussel Bathymodiolus thermophilus have been questioned. The low activities of enzymes diagnostic for CO2 fixation (Calvin cycle) and for sulfur-driven energy generation, as measured by other investigators, have been attributed to bacterial contamination of the gill surface. Based on research at the Galápagos Rift hydrothermal vents in 1988 and subsequent laboratory experiments, the current study confirms that the B. thermophilus symbiont is a psychrophile for which thiosulfate and sulfide stimulate CO2 fixation. It strongly indicates that the symbiont is a chemoautotroph by establishing the following: (1) Sulfide and thiosulfate can stimulate CO2 fixation by partially purified symbionts by up to 43-fold and 120-fold, respectively; (2) the ribulose-1,5-bisphosphate carboxylase/oxygenase activity of the symbiont is sufficient to account for its sulfide- or thiosulfate-stimulated CO2 incorporation; (3) the symbiont's molar growth yield on thiosulfate, as judged by CO2 incorporation, is indistinguishable from that of free-living chemoautotrophs. Due to the high protein-degrading activity of B. thermophilus gill lysate, it is also suggested that host lysis of symbionts plays a more important role in the nutrition of the vent mussel than in R. pachyptila or C. magnifica, for which no comparable protein-degrading activity was found.
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