Prevalence of human metapneumovirus in hospitalized children with respiratory tract infections in Tianjin, China.

Human metapneumovirus (hMPV) has recently been recognized as an important respiratory pathogen, especially in children. At present, our understanding of the characteristics of hMPV from China is very limited. Nasopharyngeal aspirates were taken from 310 hospitalized pediatric patients. Twenty (6.5%) of them were infected with hMPV, and they all developed pneumonia. Sixty five percent (13/20) of the cases were under 12 months. Phylogenetic analysis of F gene fragments indicated that three sub-genotypes of hMPV(A2a/A2b, B1,B2) circulated in Tianjin and A2b was the predominant subtype. The Vero-E6 cell line was better than LLC-MK2 for hMPV isolation. Three hMPV strains were successfully isolated using the Vero-E6 cell line.

Tetra-µ-benzoato-κO:O'-bis-[(benzoic acid-κO)nickel(II)].

The title compound, [Ni(2)(C(7)H(5)O(2))(4)(C(7)H(6)O(2))(2)], is composed of two Ni(II) ions, four bridging benzoate anions and two η(1)-benzoic acid mol-ecules. The [Ni(2)(PhCOO)(4)] unit adopts a typical paddle-wheel conformation. The center between the two Ni(II) atoms represents a crystallographic center of inversion. In addition, each Ni(II) ion also coordinates to one O atom from a benzoic acid mol-ecule. The crystal packing is realised by inter-molecular hydrogen-bonding inter-actions and π-π stacking inter-actions, with a centroid-centroid distance of 3.921 (1) Å.

Diaqua-bis(8-chloro-1,3-dimethyl-2,6-dioxo-1,2,3,6-tetra-hydro-7H-purinato-κN)copper(II) dihydrate.

The title mononuclear copper(II) complex, [Cu(C(7)H(6)ClN(4)O(2))(2)(H(2)O)(2)]·2H(2)O, based on 8-chloro-theophylline (HCt), has the Cu atom at a center of symmetry in a slightly distorted trans square-planar geometry coordinated by two N atoms of two deprotonated HCt ligands and two O atoms of water mol-ecules. The crystal packing is stabilized by hydrogen bonds involving deprotonated HCt ligands, coordinated water mol-ecules and uncoordinated solvent water mol-ecules.

Homodimerization of the c-Abl protein tyrosine kinase.

The c-Abl nonreceptor tyrosine kinase is activated in the cellular responses to genotoxic, oxidative and other forms of stress. Using tagged forms of c-Abl, the present studies demonstrate that c-Abl forms homodimers in cells. The results show that the c-Abl N-terminal regions interact with the corresponding C-terminal regions of both partners in the dimmer. Specifically, the c-Abl SH3 domain binds to a proline-rich motif at amino acids 958-982 in the c-Abl C-terminal region. Deletion of the proline-rich motif disrupts dimmer formation. These findings provide the first evidence that c-Abl forms homodimers and indicate that homodimerization can contribute to the regulation of c-Abl activity.

[Over-expression in Escherichia coli and purification of nucleocaspid and membrane protein of SARS coronavirus].

Genes encoding nucleocaspid (N) and membrane (M) protein of SARS coronavirus were obtained by RT-PCR and were cloned into expression vector pET22b and pBV222. DNA sequencing showed that the genes cloned from a patient in Beijing were identical to the gene sequences from reported Toronto strain. The genes were over-expressed in E. coli either as inclusion body or as soluble form. The recombinant proteins were purified by ion-exchange, or ion-exchange followed by metal chelate affinity chromatography. The recombinant N protein was demonstrated highly antigenic and could be employed as antigen to detect SARS antibodies in ELISA system for SARS diagnosis.