Migration routes and differences in migration strategies of Whooper Swans between spring and autumn

Long-distance migratory birds travel more rapidly in spring than in autumn,as they face temporal breeding constraints.However,several species travel slower in spring owing to environmental influences,such as food availability and wind conditions.GPS trackers were attached to 17 Whooper Swans(Cygnus cygnus) inhabiting northeastern Mongolia,to determine their migration routes and stopover sites in spring and autumn.Differences between spring and autumn migrations,migration-influencing parameters,and the effect of spring stopover site temperatures were analyzed.Six swans completed perfect tours between their wintering and breeding sites,and these data were used for analysis.Spring migration lasted 57 days,with 49.2 days spent at 3.7 stopover sites.Autumn migration lasted 21.5 days,with 17.5 days spent at 1.0 stopover sites.Thus,the swans traveled more rapidly in autumn than in spring.Migration distance,number of stopovers,migration speed,and straightness were important migration determinants in both spring and autumn.Migration distance,stopover duration,number of stopovers,daily travel speed,travel duration,and migration speed differed significantly between spring and autumn.During spring migration,the temperature at the current stopover sites and that at the future stopover sites displayed significant variations(t=1585.8,df=631.6,p <0.001).These findings are critical for the conservation and management of Whooper Swans and their key habitats in East Asian regions,and the data are anticipated to make a particularly significant contribution toward developing detailed management plans for the conservation of their key habitats.

Genetic Characteristics of 2009 Pandemic H1N1 Influenza A Viruses Isolated from China's Mainland

A total of 100 H1N1 flu real-time-PCR positive throat swabs collected from fever patients in Zhejiang, Hubei and Guangdong between June and November 2009, were provided by local CDC laboratories. After MDCK cell culture, 57 Influenza A Pandemic （H1N1） viruses were isolated and submitted for whole genome sequencing. A total of 39 HA sequences, 52 NA sequences, 36 PB2 sequences, 31 PB1 sequences, 40 PA sequences, 48 NP sequences, 51 MP sequences and 36 NS sequences were obtained, including 20 whole genome sequences. Sequence comparison revealed they shared a high degree of homology （96%-99%） with known epidemic strains （A/Califomia/04/2009（H1N1）. Phylogenetic analysis showed that although the sequences were highly conserved, they clustered into a small number of groups with only a few distinct strains. Site analysis revealed three substitutions at loop 220 （221-228） of the HA receptor binding site in the 39 HA sequences： A/Hubei/86/2009 PKVRDQEG→PKVRDQEA, A/Zhejiang/08/2009 PKVRDQEG→PKVRDQER, A/Hubei/75/2009 PKVRDQEG→PKVRDQGG, the A/Hubei/75/2009 was isolated from an acute case, while the other two were from patients with mild symptoms. Other key sites such as 119, 274, 292 and 294 amino acids of NA protein,627 of PB2 protein were conserved. Meanwhile, all the M2 protein sequences possessed the Ser32Asn mutation, suggesting that these viruses were resistant to adamantanes. Comparison of these sequences with other H1N1 viruses collected from the NCBI database provides insight into H1N1 transmission and circulation patterns.

Site-specific determination of TTR-related functional peptides by using scanning tunneling microscopy

For the design and optimization of functional peptides, unravelling the structures of individual building blocks as well as the properties of the ensemble is paramount. TI＇R1, derived from human transthyretin, is a fibril-forming peptide implicated in diseases such as familial amyloid polyneuropathy and senile systemic amyloidosis. The functional peptide TTR1-RGD, based on a TFR1 scaffold, was designed to specifically interact with cells. Here, we used scanning tunneling microscopy （STM） to analyze the assembly structures of TTRl-related peptides with both the reverse sequence and the modified forward sequence. The site- specific analyses show the following： i） The TIR1 peptide is involved in assembly, nearly covering the entire length within the ordered [3-sheet structures, ii） For TTR1-RGD peptide assemblies, the TTR1 motif forms the ordered [3-sheet while the RGDS motif adopts a flexible conformation allowing it to promote cell adhesion. The key site is clearly identified as the linker residue Gly13. iii） Close inspection of the forward and reverse peptide assemblies show that in spite of the difference in chemistry, they display similar assembling characteristics, illustrating the robust nature of these peptides, iv） Glycine linker residues are included in the ^-strands, which strongly suggests that the sequence could be optimized by adding more linker residues. These garnered insights into the assembled structures of these peptides help unravel the mechanism driving peptide assemblies and instruct the rational design and optimization of sequence- programmed peptide architectures.