滦河上游——白枕鹤西部种群的重要停歇地

白枕鹤(Grus vipio)为国家II级重点保护野生动物, 被IUCN列为易危(VU)物种。白枕鹤西部种群繁殖于中蒙俄交界处的达乌尔地区, 数量呈下降趋势。我们于2017-2018年在蒙古国东部给白枕鹤西部种群的50只个体佩戴了GPS-GSM跟踪设备。截至2019年5月, 获得春季和秋季迁徙路径各48条。分析结果显示: 春季91.67%和秋季72.91%的跟踪个体在滦河上游(河北省沽源-内蒙古正蓝旗-多伦区域)停歇, 春季停留时间36.16 ± 15.00天、秋季20.26 ± 11.08天, 分别占春季和秋季迁徙时间的75%和67%, 确定了这一区域是西部种群迁徙途中最重要的停歇地。迁徙路线栖息地选择模型结果显示, 白枕鹤常在距离湖泊较近(< 210 km)、海拔1,200-1,500 m, 且坡度小(< 1°)的区域停歇。而滦河上游和整条迁徙路线停歇位点比较的模型结果显示, 滦河上游停歇地的海拔1,200-1,500 m与整条迁徙路线栖息地选择模型的结果一致; 此外这个区域离河流更近(< 70 km), 不仅有湿地和水体的栖息环境, 还有草地和农田可供觅食和栖息。保护空缺分析发现滦河上游现有四处保护地, 但在保护地内的迁徙停歇点不超过总位点的1.63%。综上, 我们建议将滦河上游整体纳入保护地体系进行管理, 为这一受胁物种及其栖息地管理和保护提供可靠保障。     

Cranial suture morphometry and mechanical response to loading: 2D vs. 3D assumptions and characterization

Biomechanics and Modeling in Mechanobiology - Cranial sutures are complex soft tissue structures whose mechanics are often studied due to their link with bone growth in the skull. Researchers will...     

Little Evidence of Avian or Equine Influenza Virus Infection among a Cohort of Mongolian Adults with Animal Exposures, 2010–2011

Avian (AIV) and equine influenza virus (EIV) have been repeatedly shown to circulate among Mongolia’s migrating birds or domestic horses. In 2009, 439 Mongolian adults, many with occupational exposure to animals, were enrolled in a prospective cohort study of zoonotic influenza transmission. Sera were drawn upon enrollment and again at 12 and 24 months. Participants were contacted monthly for 24 months and queried regarding episodes of acute influenza-like illnesses (ILI). Cohort members confirmed to have acute influenza A infections, permitted respiratory swab collections which were studied with rRT-PCR for influenza A. Serologic assays were performed against equine, avian, and human influenza viruses. Over the 2 yrs of follow-up, 100 ILI investigations in the cohort were conducted. Thirty-six ILI cases (36%) were identified as influenza A infections by rRT-PCR; none yielded evidence for AIV or EIV. Serological examination of 12 mo and 24 mo annual sera revealed 37 participants had detectable antibody titers (≥1∶10) against studied viruses during the course of study follow-up: 21 against A/Equine/Mongolia/01/2008(H3N8); 4 against an avian A/Teal/Hong Kong/w3129(H6N1), 11 against an avian-like A/Hong Kong/1073/1999(H9N2), and 1 against an avian A/Migrating duck/Hong Kong/MPD268/2007(H10N4) virus. However, all such titers were <1∶80 and none were statistically associated with avian or horse exposures. A number of subjects had evidence of seroconversion to zoonotic viruses, but the 4-fold titer changes were again not associated with avian or horse exposures. As elevated antibodies against seasonal influenza viruses were high during the study period, it seems likely that cross-reacting antibodies against seasonal human influenza viruses were a cause of the low-level seroreactivity against AIV or EIV. Despite the presence of AIV and EIV circulating among wild birds and horses in Mongolia, there was little evidence of AIV or EIV infection in this prospective study of Mongolians with animal exposures.     

Super Secondary Structure Consisting of a Polyproline II Helix and a β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors

Leucine rich repeats (LRRs) are present in over 100,000 proteins from viruses to eukaryotes. The LRRs are 20–30 residues long and occur in tandem. LRRs form parallel stacks of short β-strands and then assume a super helical arrangement called a solenoid structure. Individual LRRs are separated into highly conserved segment (HCS) with the consensus of LxxLxLxxNxL and variable segment (VS). Eight classes have been recognized. Bacterial LRRs are short and characterized by two prolines in the VS; the consensus is xxLPxLPxx with Nine residues (N-subtype) and xxLPxxLPxx with Ten residues (T-subtype). Bacterial LRRs are contained in type III secretion system effectors such as YopM, IpaH3/9.8, SspH1/2, and SlrP from bacteria. Some LRRs in decorin, fribromodulin, TLR8/9, and FLRT2/3 from vertebrate also contain the motifs. In order to understand structural features of bacterial LRRs, we performed both secondary structures assignments using four programs—DSSP-PPII, PROSS, SEGNO, and XTLSSTR—and HELFIT analyses (calculating helix axis, pitch, radius, residues per turn, and handedness), based on the atomic coordinates of their crystal structures. The N-subtype VS adopts a left handed polyproline II helix (PPII) with four, five or six residues and a type I β-turn at the C-terminal side. Thus, the N-subtype is characterized by a super secondary structure consisting of a PPII and a β-turn. In contrast, the T-subtype VS prefers two separate PPIIs with two or three and two residues. The HELFIT analysis indicates that the type I β-turn is a right handed helix. The HELFIT analysis determines three unit vectors of the helix axes of PPII (P), β-turn (B), and LRR domain (A). Three structural parameters using these three helix axes are suggested to characterize the super secondary structure and the LRR domain.