The Importance of Time Congruity in the Organisation.

In 1991 Kaufman, Lane, and Lindquist proposed that time congruity in terms of an individual's time preferences and the time use methods of an organisation would lead to satisfactory performance and enhancement of quality of work and general life. The research reported here presents a study which uses commensurate person and job measures of time personality in an organisational setting to assess the effects of time congruity on one aspect of work life, job-related affective well-being. Results show that time personality and time congruity were found to have direct effects on well-being and the influence of time congruity was found to be mediated through time personality, thus contributing to the person–job (P–J) fit literature which suggests that direct effects are often more important than indirect effects. The study also provides some practical examples of ways to address some of the previously cited methodological issues in P–J fit research

From marine bands to hybrid flows: sedimentology of a Mississippian black shale

Organic‐rich mudstones have long been of interest as conventional and unconventional source rocks and are an important organic carbon sink. Yet the processes that deposited organic‐rich muds in epicontinental seaways are poorly understood, partly because few modern analogues exist. This study investigates the processes that transported and deposited sediment and organic matter through part of the Bowland Shale Formation, from the Mississippian Rheic–Tethys seaway. Field to micron‐scale sedimentological analysis reveals a heterogeneous succession of carbonate‐rich, siliceous, and siliciclastic, argillaceous muds. Deposition of these facies at basinal and slope locations was moderated by progradation of the nearby Pendle delta system, fourth‐order eustatic sea‐level fluctuation and localized block and basin tectonism. Marine transgressions deposited bioclastic ‘marine band’ (hemi)pelagic packages. These include abundant euhaline macrofaunal tests, and phosphatic concretions of organic matter and radiolarian tests interpreted as faecal pellets sourced from a productive water column. Lens‐rich (lenticular) mudstones, hybrid, debrite and turbidite beds successively overlie marine band packages and suggest reducing basin accommodation promoted sediment deposition via laminar and hybrid flows sourced from the basin margins. Mud lenses in lenticular mudstones lack organic linings and bioclasts and are equant in early‐cemented lenses and in plan‐view, and are largest and most abundant in mudstones overlying marine band packages. Thus, lenses likely represent partially consolidated mud clasts that were scoured and transported in bedload from the shelf or proximal slope, as a ‘shelf to basin’ conveyor, during periods of reduced basin accommodation. Candidate in situ microbial mats in strongly lenticular mudstones, and as rip‐up fragments in the down‐dip hybrid beds, suggest that these were potentially key biostabilizers of mud. Deltaic mud export was fast, despite the intrabasinal complexity, likely an order of magnitude higher than similar successions deposited in North America. Epicontinental basins remotely linked to delta systems were therefore capable of rapidly accumulating both sediment and organic matter

Inactivation of White Spot Syndrome Virus (WSSV) by normal rabbit serum: Implications for the role of the envelope protein VP28 in WSSV infection of shrimp

White Spot Syndrome Virus (WSSV) is a highly pathogenic and prevalent virus affecting crustacea. A number of WSSV envelope proteins, including vp28, have been proposed to be involved in viral infectivity based on the ability of specific antibodies to attenuate WSSV-induced mortality in vivo. In the present study, a series of monoclonal and polyclonal antibodies targeting vp28 were tested for their ability to neutralize WSSV infectivity, with the purpose of identifying epitopes potentially involved in vp28-mediated infection of shrimp. Surprisingly, when used as protein A-purified immunoglobulin, none of the antibodies tested were capable of inhibiting WSSV infectivity. This included one polyclonal preparation that has been previously shown to inactivate WSSV, when used as whole rabbit serum. Moreover, strong inactivation of WSSV by some rabbit sera was observed, in a manner independent of anti-vp28 antibodies. These results underscore the problems associated with using heterogeneous reagents (e.g. whole rabbit antiserum) in viral neutralization experiments aimed at defining proteins involved in infection by WSSV. In light of this, the potential of anti-vp28 antibodies to specifically neutralize WSSV should be reconsidered

Influence of the μ-chain C-terminal sequence on polymerization of immunoglobulin M

Immunoglobulin (IgM) is found in various states of covalent polymerization (μL)n, where n is typically 8, 10, or 12. The usual form of IgM of bony fish is tetrameric (8 μL units) as compared to the pentameric form (10 μL units) observed in cartilaginous fish and mammals. Two hypotheses were tested in this study. First, that the length of the μ-chain C terminus following Cys575 determines whether an IgM polymerizes as a tetramer or as a pentamer. This was tested by examining the covalent polymerization state of mouse IgM mutated to contain a series of μ-chain C-termini from bony and cartilaginous fish. The results proved this hypothesis wrong: mouse IgM bearing the C-terminal sequence of shark, salmon and cod μ-chain behaved identically to native mouse IgM, forming predominantly (μL)10 and (μL)12 forms. The second hypothesis was that an additional Cys residue near the C terminus of the μ-chain is responsible for the multiple covalent structures seen in IgM of the channel catfish. The addition of a catfish C terminus to the mouse μ-chain resulted, as predicted, in the production of a series of covalently bonded forms, with the major species being (μL)4. When a Ser-Cys unit was removed from the catfish C terminus added to the mouse μ-chain, this resulted in production of IgM indistinguishable in structure from that of wild-type mouse IgM