Background:The carbohydrate specificity of the oyster galectin CvGal1 for endogenous and exogenous glycans was unresolved. Results: CvGal1 recognizes blood group A tetrasaccharides on oyster hemocytes, which are absent on the surface of the P. marinus parasite. Conclusion: Oyster hemocytes and P. marinus display structurally distinct ligands for CvGal1. Significance: Galectins may function as pattern recognition receptors by binding microbial glycans structurally different from endogenous ligands.

Background: M. tuberculosis

Music can be a particularly effective cue for bringing one back to the sights and sounds of events from across the lifespan. These music-evoked autobiographical memories (MEAMs) have typically been studied within laboratory experiments and clinical settings, often using experimenter-selected music to cue autobiographical memories. The present work took a more naturalistic approach, by studying the situational aspects, contents, and features of MEAMs within the course of participants’ everyday lives. Participants ( N = 31) recorded details of their MEAMs and music listening habits in a diary for 7 days. MEAMs were experienced, on average, once per day and were cued by a wide variety of music, often during routine tasks such as traveling and housework. Everyday MEAMs were typically rated as highly vivid and involuntary and were often accompanied by positive or mixed emotions (e.g., happiness, nostalgia) and social themes. Some evidence of individual differences was found, with older participants rating their MEAMs as more vivid and accompanied by more positive emotions. The features reported within everyday MEAMs replicated several previous findings on MEAMs and autobiographical memory more generally, indicating that this naturalistic method was able to capture genuine MEAM experiences. Implications for future research on naturally occurring MEAMs are discussed.

The Escherichia coli Ppx protein is an exopolyphosphatase that degrades long-chain polyphosphates in a highly processive reaction. It also hydrolyzes the terminal 5' phosphate of the modified nucleotide guanosine 5' triphosphate 3' diphosphate (pppGpp). The structure of Ppx has been determined to 1.9 A resolution by X-ray crystallography. The exopolyphosphatase is an ASKHA (acetate and sugar kinases, Hsp70, actin) phosphotransferase with an active site found in a cleft between the two amino-terminal domains. Analysis of the active site indicates that among the ASKHA phosphotranferases of known structure, Ppx is the closest to the ectonucleoside triphosphate diphosphohydrolases. A third domain forms a six-helix claw that is similar to the catalytic core of the eukaryotic cyclic nucleotide phosphodiesterases. Most of the 29 sulfate ions bound to the Ppx dimer occupy sites where the polyP chain likely binds. An aqueduct that passes through the enzyme provides a physical basis for the enzyme's high processivity.