@article {Ott2004b,
	title = {{Symbioses between Marine N ematodes and Sulfur-oxidizing Chemoautotrophic Bacteria}},
	journal = {Symbiosis},
	volume = {36},
	year = {2004},
	pages = {103{\textendash}126},
	keywords = {chemoautotrophic bacteria, meiofauna, nematodes, sulfide system, Symbiosis},
	author = {Ott, J{\"o}rg and Bright, Monika and Bulgheresi, Silvia}
}
@article {Pende2014,
	title = {{Size-independent symmetric division in extraordinarily long cells}},
	journal = {Nature Communications},
	volume = {5},
	year = {2014},
	month = {sep},
	pages = {4803},
	issn = {2041-1723},
	doi = {10.1038/ncomms5803},
	url = {http://www.nature.com/doifinder/10.1038/ncomms5803},
	author = {Pende, Nika and Leisch, Nikolaus and Gruber-Vodicka, Harald R. and Heindl, Niels R. and Ott, J{\"o}rg and den Blaauwen, Tanneke and Bulgheresi, Silvia}
}
@article {Leisch,
	title = {{Growth in width and FtsZ ring longitudinal positioning in a gamma - proteobacterial symbiont}},
	journal = {Current Biology},
	volume = {22},
	number = {19},
	year = {Submitted},
	pages = {R831{\textendash}R832},
	author = {Leisch, Nikolaus and Verheul, Jolanda and Heindl, Niels R and Gruber-Vodicka, Harald R and Pende, Nika and Blaauwen, Tanneke Den and Bulgheresi, Silvia}
}
@article {Nabatov2008,
	title = {{C-type lectin Mermaid inhibits dendritic cell mediated HIV-1 transmission to CD4+ T cells.}},
	journal = {Virology},
	volume = {378},
	number = {2},
	year = {2008},
	month = {sep},
	pages = {323{\textendash}8},
	publisher = {Elsevier Inc.},
	abstract = {Dendritic cells (DCs) are important in HIV-1 transmission; DCs capture invading HIV-1 through the interaction of the gp120 oligosaccharides with the C-type lectin DC-SIGN and migrate to the lymphoid tissues where HIV-1 is transmitted to T cells. Thus, the HIV-1 envelope glycoprotein gp120 is an attractive target to prevent interactions with DCs and subsequent viral transmission. Here, we have investigated whether the structural homologue of DC-SIGN, the nematode C-type lectin Mermaid can be used to prevent HIV-1 transmission by DCs. Our data demonstrate that Mermaid interacts with high mannose structures present on HIV-1 gp120 and thereby inhibits HIV-1 binding to DC-SIGN on DCs. Moreover, Mermaid inhibits DC-SIGN-mediated HIV-1 transmission from DC to T cells. We have identified Mermaid as a non-cytotoxic agent that shares the glycan specificity with DC-SIGN and inhibits DC-SIGN-gp120 interaction. The results are important for the anti-HIV-1 microbicide development directed at preventing DC-HIV-1 interactions.},
	keywords = {Animals, Anti-HIV Agents, Anti-HIV Agents: pharmacology, C-Type, C-Type: metabolism, CD4-Positive T-Lymphocytes, CD4-Positive T-Lymphocytes: virology, Cell Adhesion Molecules, Cell Adhesion Molecules: metabolism, Cell Line, Cell Surface, Cell Surface: metabolism, Cells, Cultured, Dendritic Cells, Dendritic Cells: virology, Helminth Proteins, Helminth Proteins: pharmacology, Helminth Proteins: toxicity, HIV Envelope Protein gp120, HIV Envelope Protein gp120: metabolism, HIV-1, HIV-1: drug effects, Humans, Lectins, Nematoda, Protein Binding, Receptors, Virus Attachment},
	issn = {1096-0341},
	doi = {10.1016/j.virol.2008.05.025},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/18597806},
	author = {Nabatov, Alexey a and de Jong, Marein a W P and de Witte, Lot and Bulgheresi, Silvia and Geijtenbeek, Teunis B H}
}
@article {Heindl2011,
	title = {{First detection of thiotrophic symbiont phylotypes in the pelagic marine environment.}},
	journal = {FEMS microbiology ecology},
	volume = {77},
	number = {1},
	year = {2011},
	month = {jul},
	pages = {223{\textendash}7},
	abstract = {Marine oligochaete and nematode thiotrophic symbionts (MONTS) form a phylogenetic cluster within the Gammaproteobacteria. For the symbionts that live on the nematode surface, environmental transmission is likely. However, until now, no free-living relatives have been found. In this study, we detected MONTS cluster members in offshore surface seawater of both the Caribbean and the Mediterranean Sea by PCR amplification of their 16S rRNA genes. This is the first evidence of members of this cluster in the pelagic environment. These may either be free-living forms of the symbionts or closely related, nonsymbiotic strains. In either case, their existence sheds light on the evolution of beneficial symbioses between shallow water invertebrates and sulfur-oxidizing bacteria.},
	keywords = {16S, 16S: genetics, Animals, Bacterial, Biological Evolution, Caribbean Region, Gammaproteobacteria, Gammaproteobacteria: classification, Gammaproteobacteria: genetics, Genes, Mediterranean Sea, Molecular Sequence Data, Nematoda, Nematoda: microbiology, Phylogeny, Ribosomal, RNA, Seawater, Seawater: microbiology, Symbiosis},
	issn = {1574-6941},
	doi = {10.1111/j.1574-6941.2011.01096.x},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/21434948},
	author = {Heindl, Niels R and Gruber-Vodicka, Harald R and Bayer, Christoph and L{\"u}cker, Sebastian and Ott, J and Bulgheresi, Silvia}
}
@article {Bayer2009,
	title = {{Molecular characterization of the symbionts associated with marine nematodes of the genus Robbea}},
	journal = {Environmental Microbiology Reports},
	volume = {1},
	number = {2},
	year = {2009},
	pages = {136{\textendash}144},
	keywords = {Belize, Caribbean Sea, Cayman Islands, Corsica, Description, Mediterranean Sea, Robbea, Stilbonematinae},
	author = {Bayer, C and Heindl, N R and Rinke, C and L{\"u}cker, Sebastian and Ott, J and Bulgheresi, Silvia}
}
@article {Bulgheresi2011,
	title = {{Calling the roll on Laxus oneistus immune defense molecules.}},
	journal = {Symbiosis (Philadelphia, Pa.)},
	volume = {55},
	number = {3},
	year = {2011},
	month = {nov},
	pages = {127{\textendash}135},
	issn = {0334-5114},
	doi = {10.1007/s13199-012-0157-3},
	url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3294214{\&}tool=pmcentrez{\&}rendertype=abstract},
	author = {Bulgheresi, Silvia}
}
@article {Bulgheresi2011a,
	title = {{Sequence variability of the pattern recognition receptor Mermaid mediates specificity of marine nematode symbioses.}},
	journal = {The ISME journal},
	volume = {5},
	number = {6},
	year = {2011},
	month = {jun},
	pages = {986{\textendash}98},
	publisher = {Nature Publishing Group},
	abstract = {Selection of a specific microbial partner by the host is an all-important process. It guarantees the persistence of highly specific symbioses throughout host generations. The cuticle of the marine nematode Laxus oneistus is covered by a single phylotype of sulfur-oxidizing bacteria. They are embedded in a layer of host-secreted mucus containing the mannose-binding protein Mermaid. This Ca(2+)-dependent lectin mediates symbiont aggregation and attachment to the nematode. Here, we show that Stilbonema majum-a symbiotic nematode co-occurring with L. oneistus in shallow water sediment-is covered by bacteria phylogenetically distinct to those covering L. oneistus. Mermaid cDNA analysis revealed extensive protein sequence variability in both the nematode species. We expressed three recombinant Mermaid isoforms, which based on the structural predictions display the most different carbohydrate recognition domains (CRDs). We show that the three CRDs (DNT, DDA and GDA types) possess different affinities for L. oneistus and S. majum symbionts. In particular, the GDA type, exclusively expressed by S. majum, displays highest agglutination activity towards its symbionts and lowest towards its L. oneistus symbionts. Moreover, incubation of L. oneistus in the GDA type does not result in complete symbiont detachment, whereas incubation in the other types does. This indicates that the presence of particular Mermaid isoforms on the nematode surface has a role in the attachment of specific symbionts. This is the first report of the functional role of sequence variability in a microbe-associated molecular patterns receptor in a beneficial association.},
	keywords = {16S, 16S: genetics, Amino Acid Sequence, Animals, Bacteria, Bacteria: classification, Bacteria: genetics, Bacteria: isolation {\&} purification, Bacterial Physiological Phenomena, Helminth Proteins, Helminth Proteins: chemistry, Mannose-Binding Lectin, Mannose-Binding Lectin: chemistry, Mannose-Binding Lectins, Mannose-Binding Lectins: genetics, Models, Molecular, Molecular Sequence Data, Nematoda, Nematoda: genetics, Nematoda: microbiology, Nematoda: physiology, Pattern Recognition, Pattern Recognition: chemistry, Phylogeny, Protein Isoforms, Protein Isoforms: chemistry, Receptors, Ribosomal, RNA, Sequence Alignment, Symbiosis},
	issn = {1751-7370},
	doi = {10.1038/ismej.2010.198},
	url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3131856{\&}tool=pmcentrez{\&}rendertype=abstract},
	author = {Bulgheresi, Silvia and Gruber-Vodicka, Harald R and Heindl, Niels R and Dirks, Ulrich and Kostadinova, Maria and Breiteneder, Heimo and Ott, J}
}
@article {Bulgheresi2006,
	title = {{A new C-type lectin similar to the human immunoreceptor DC-SIGN mediates symbiont acquisition by a marine nematode}},
	journal = {Applied and Enviromental Microbiology},
	volume = {72},
	number = {4},
	year = {2006},
	pages = {2950{\textendash}2956},
	doi = {10.1128/AEM.72.4.2950},
	url = {http://aem.asm.org/content/72/4/2950.short},
	author = {Bulgheresi, Silvia and Schabussova, Irma and Chen, T and Mullin, N P and Maizels, R M and Ott, J}
}
