The Polonnaruwa meteorite: oxygen isotope, crystalline and biological composition

Results of X-Ray Diffraction (XRD) analysis, Triple Oxygen Isotope analysis and Scanning Electron Microscopic (SEM) studies are presented for stone fragments recovered from the North Central Province of Sri Lanka following a witnessed fireball event on 29 December 2012. The existence of numerous nitrogen depleted highly carbonaceous fossilized biological structures fused into the rock matrix is inconsistent with recent terrestrial contamination. Oxygen isotope results compare well with those of CI and CI-like chondrites but are inconsistent with the fulgurite hypothesis.Comment: 7 pages, 7 figures, 4 table

Engineering novel complement activity into a pulmonary surfactant protein

Complement neutralizes invading pathogens, stimulates inflammatory and adaptive immune responses, and targets non- or altered-self structures for clearance. In the classical and lectin activation pathways, it is initiated when complexes composed of separate recognition and activation subcomponents bind to a pathogen surface. Despite its apparent complexity, recognition-mediated activation has evolved independently in three separate protein families, C1q, mannose-binding lectins (MBLs), and serum ficolins. Although unrelated, all have bouquet-like architectures and associate with complement-specific serine proteases: MBLs and ficolins with MBL-associated serine protease-2 (MASP-2) and C1q with C1r and C1s. To examine the structural requirements for complement activation, we have created a number of novel recombinant rat MBLs in which the position and orientation of the MASP-binding sites have been changed. We have also engineered MASP binding into a pulmonary surfactant protein (SP-A), which has the same domain structure and architecture as MBL but lacks any intrinsic complement activity. The data reveal that complement activity is remarkably tolerant to changes in the size and orientation of the collagenous stalks of MBL, implying considerable rotational and conformational flexibility in unbound MBL. Furthermore, novel complement activity is introduced concurrently with MASP binding in SP-A but is uncontrolled and occurs even in the absence of a carbohydrate target. Thus, the active rather than the zymogen state is default in lectin·MASP complexes and must be inhibited through additional regions in circulating MBLs until triggered by pathogen recognition

Training problems in community development: a proposal for research

The I.D.S. SRDP evaluation concludes that not enough attention has yet been paid to the promotion and guidance of participation in self-help activities. In particular, it was felt that more effort was required for “training” leaders for these activities. This research proposal takes its cue from this perspective. It is concerned with evaluating what is at present being done in the field of training at different levels, probably with special reference to the Community development assistants, Chiefs and local project committee leaders. It is hypothesised that there are a number of constraints upon CD training. Five main ones are suggested:- a) the tendency for bureaucratic organisations to encourage conformity, rather than innovativeness; b) the difficulty of establishing and maintaining cooperation between different agencies who are involved in CD in the field; c) the likelihood that the Chiefs, who play an important role in CD, may not be oriented to the participatory ideas which theoretically guide the ‘harambee’ movement; d) the lack of clear objectives which can guide field officers involved in CD training; e) the difficulty of establishing harmonious relationships between CD and actors within the political system. The research will be mainly carried out in SRDP areas (although non-SRDP areas may provide useful comparative data). A Questionnaire will be administered, but more importance is attached to the in-depth interview and participant-observation

Paths reunited: initiation of the classical and lectin pathways of complement activation

Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since its isolation almost 50 years ago. Nevertheless, knowledge is still incomplete, especially with regard to the interactions between its subcomponents C1q, C1r and C1s that trigger activation upon binding to a microbial target. Recent studies have provided new insights into these interactions, and have revealed unexpected parallels with initiating complexes of the lectin pathway of complement: MBL–MASP and ficolin–MASP. Here, we develop and expand these concepts and delineate their implications towards the key aspects of complement activation via the classical and lectin pathways

The backbone of Africa

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