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PubMed:15316015 JSONTXT 25 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-170 Sentence denotes Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae: oligomerization of IncA mediates interaction between facing membranes.
T2 171-265 Sentence denotes The developmental cycle of Chlamydiaceae occurs in a membrane compartment called an inclusion.
T3 266-372 Sentence denotes IncA is a member of a family of proteins synthesized and secreted onto the inclusion membrane by bacteria.
T4 373-459 Sentence denotes IncA proteins from different species of Chlamydiaceae show little sequence similarity.
T5 460-562 Sentence denotes We report that the biochemical properties of Chlamydia trachomatis and Chlamydia caviae are conserved.
T6 563-610 Sentence denotes Both proteins self-associate to form multimers.
T7 611-700 Sentence denotes When artificially expressed by the host cell, they localize to the endoplasmic reticulum.
T8 701-828 Sentence denotes Strikingly, heterologous expression of IncA in the endoplasmic reticulum completely inhibits concomitant inclusion development.
T9 829-1054 Sentence denotes Using truncated forms of IncA from C. caviae, we show that expression of the C-terminal cytoplasmic domain of the protein at the surface of the endoplasmic reticulum is sufficient to disrupt the bacterial developmental cycle.
T10 1055-1360 Sentence denotes On the other hand, development of a C. trachomatis strain that does not express IncA is not inhibited by artificial IncA expression, showing that the disruptive effect observed with the wild-type strain requires direct interactions between IncA molecules at the inclusion and on the endoplasmic reticulum.
T11 1361-1542 Sentence denotes Finally, we modeled IncA tetramers in parallel four helix bundles based on the structure of the SNARE complex, a conserved structure involved in membrane fusion in eukaryotic cells.
T12 1543-1625 Sentence denotes Both C. trachomatis and C. caviae IncA tetramers were highly stable in this model.
T13 1626-1874 Sentence denotes In conclusion, we show that the property of IncA proteins to assemble into multimeric structures is conserved between chlamydial species, and we propose that these proteins may have co-evolved with the SNARE machinery for a role in membrane fusion.