The kinematics of swimming and relocation jumps in copepod nauplii

Copepod nauplii move in a world dominated by viscosity. Their swimming-by-jumping propulsion mode, with alternating power and recovery strokes of three pairs of cephalic appendages, is fundamentally different from the way other microplankters move. Protozoans move using cilia or flagella, and copepodites are equipped with highly specialized swimming legs. In some species the nauplius may also propel itself more slowly through the water by beating and rotating the appendages in a different, more complex pattern. We use high-speed video to describe jumping and swimming in nauplii of three species of pelagic copepods: Temora longicornis, Oithona davisae and Acartia tonsa. The kinematics of jumping is similar between the three species. Jumps result in a very erratic translation with no phase of passive coasting and the nauplii move backwards during recovery strokes. This is due to poorly synchronized recovery strokes and a low beat frequency relative to the coasting time scale. For the same reason, the propulsion efficiency of the nauplii is low. Given the universality of the nauplius body plan, it is surprising that they seem to be inefficient when jumping, which is different from the very efficient larger copepodites. A slow-swimming mode is only displayed by T. longicornis. In this mode, beating of the appendages results in the creation of a strong feeding current that is about 10 times faster than the average translation speed of the nauplius. The nauplius is thus essentially hovering when feeding, which results in a higher feeding efficiency than that of a nauplius cruising through the water

Complement C1 Esterase Inhibitor Levels Linked to Infections and Contaminated Heparin-Associated Adverse Events

Activation of kinin-kallikrein and complement pathways by oversulfated-chondroitin-sulfate (OSCS) has been linked with recent heparin-associated adverse clinical events. Given the fact that the majority of patients who received contaminated heparin did not experience an adverse event, it is of particular importance to determine the circumstances that increase the risk of a clinical reaction. In this study, we demonstrated by both the addition and affinity depletion of C1inh from normal human plasma, that the level of C1inh in the plasma has a great impact on the OSCS-induced kallikrein activity and its kinetics. OSCS-induced kallikrein activity was dramatically increased after C1inh was depleted, while the addition of C1inh completely attenuated kallikrein activity. In addition, actual clinical infection can lead to increased C1inh levels. Plasma from patients with sepsis had higher average levels of functional C1inh and decreased OSCS-induced kallikrein activity. Lastly, descriptive data on adverse event reports suggest cases likely to be associated with contaminated heparin are inversely correlated with infection. Our data suggest that low C1inh levels can be a risk factor and high levels can be protective. The identification of risk factors for contact system-mediated adverse events may allow for patient screening and clinical development of prophylaxis and treatments

Chemical inhibition of bacterial protein tyrosine phosphatase suppresses capsule production

Capsule polysaccharide is a major virulence factor for a wide range of bacterial pathogens, including Streptococcus pneumoniae. The biosynthesis of Wzy-dependent capsules in both Gram-negative and –positive bacteria is regulated by a system involving a protein tyrosine phosphatase (PTP) and a protein tyrosine kinase. However, how the system functions is still controversial. In Streptococcus pneumoniae, a major human pathogen, the system is present in all but 2 of the 93 serotypes found to date. In order to study this regulation further, we performed a screen to find inhibitors of the phosphatase, CpsB. This led to the observation that a recently discovered marine sponge metabolite, fascioquinol E, inhibited CpsB phosphatase activity both in vitro and in vivo at concentrations that did not affect the growth of the bacteria. This inhibition resulted in decreased capsule synthesis in D39 and Type 1 S. pneumoniae. Furthermore, concentrations of Fascioquinol E that inhibited capsule also lead to increased attachment of pneumococci to a macrophage cell line, suggesting that this compound would inhibit the virulence of the pathogen. Interestingly, this compound also inhibited the phosphatase activity of the structurally unrelated Gram-negative PTP, Wzb, which belongs to separate family of protein tyrosine phosphatases. Furthermore, incubation with Klebsiella pneumoniae¸ which contains a homologous phosphatase, resulted in decreased capsule synthesis. Taken together, these data provide evidence that PTPs are critical for Wzydependent capsule production across a spectrum of bacteria, and as such represents a valuable new molecular target for the development of anti-virulence antibacterials.Alistair J. Standish, Angela A. Salim, Hua Zhang, Robert J. Capon and Renato Moron