In addition, the suspected relationship between increasing rates of childhood obesity and the apparent reduction in the age of puberty onset in girls has generated a growing interest in identifying the mechanisms by which nutrition may influence reproductive maturation. This review will focus on recent data unveiling the sites of leptin action in pubertal development that were generated using novel molecular techniques and genetically engineered mouse models. It will also emphasize areas of contention and the many relevant questions that remain unanswered.”
“Rift Valley

fever (RVF) is a mosquito-borne zoonotic disease caused by a phlebovirus of the family Bunyaviridae, which affects humans and ruminants in Africa and the Middle East. RFV virus see more (RVFV) possesses a single-stranded tripartite RNA genome of negative/ambisense polarity. The S segment utilizes the ambisense strategy and codes for two proteins, the N nucleoprotein and the nonstructural NSs protein, in opposite orientations. The two open reading frames (ORFs) are separated by an intergenic region (IGR) highly conserved among strains and containing a motif, 5′-GCUGC-3′, present on the genome and antigenome, which was shown previously to play a role in transcription termination (C. G. Albarino, B. H. Bird, and Selleck Ruboxistaurin S. T. Nichol, J. Virol. 81: 5246-5256,

2007; T. Ikegami, S. Won, C. J. Peters, and S. Makino, J. Virol. 81: 8421-8438, 2007). Here, we created recombinant RVFVs with mutations or deletions in the IGR and showed that the substitution of the motif sequence by a series of five A’s inactivated transcription termination at the wild-type site but allowed the transcriptase to recognize another site with the consensus sequence present in the opposite ORF. Similar situations were observed for mutants in which the motif was still present in the IGR but located close to the stop codon of the translated ORF, supporting a model in which transcription is coupled to translation and translocating ribosomes abrogate transcription termination. Our data also showed that the signal tolerated

some sequence variations, since mutation into 5′-GCAGC-3′ was functional, and 5′-GUAGC-3′ is likely the signal for the termination of the 3′ end of the L mRNA.”
“The hemagglutinin-neuraminidase GANT61 nmr (HN) protein of human parainfluenza viruses (hPIVs) both binds (H) and cleaves (N) oligosaccharides that contain N-acetylneuraminic acid (Neu5Ac). H is thought to correspond to receptor binding and N to receptor-destroying activity. At present, N’s role in infection remains unclear: does it destroy only receptors, or are there other targets? We previously demonstrated that hPIV1 and 3 HNs bind to oligosaccharides containing the motif Neu5Ac alpha 2-3Gal beta 1-4GlcNAc (M. Amonsen, D. F. Smith, R. D. Cummings, and G. M. Air, J. Virol. 81: 8341-8345, 2007).