Employ ductus venous blood flow in the early detection of trisomy 21, trisomy 18, and trisomy 13: A meta-analysis.

BACKGROUND AND OBJECTIVE: Ductus venosus (DV) Doppler has been suggested as a biomarker for the early screening of trisomy diseases. However, results from different studies have been largely inconsistent. This study aimed to investigate the relationship between DV and top 3 fetal aneuploidies by a systematical meta-analysis: trisomy 21 (T21), trisomy 18 (T18), and trisomy 13 (T13). METHODS: We performed a literature search covering articles from Medline, PubMed, RePORTER, and Elsevier publications. DV-T21/T18/T13 relation data were extracted from 9, 7, and 6 previous studies, respectively, including 31,053, 28,092 and 26,721 pregnant women worldwide. Both random-effects and fixed-effect model were used to study the log odds ratio (LOR) of T21, T18, and T13 in case of DV. Four potential influential factors were studied using a multiple linear regression (MLR) model, including maternal age, data age, sample size, and population region. RESULTS: DV was significantly related to T21, T18, and T13 (LOR = 3.44, 3.89 and 3.46; P value <2.1E-13). Significant between-study variance was observed for T21 (P value <1.71E-14), but not for T18 (P value >.05) and T13 (P value >.87). MLR results suggested that significant influential factors could include population region (P value <.0021), but not sample size, data age, and maternal age (P value >.078). CONCLUSIONS: Integrating DV could help in the detection of trisomy. However, accuracy and validity may vary depending on the population regions, which need further study.

[Constructing a phage-displayed random mutation library of HIV-1 Tat38-61 at the sites of 51 and 55 amino acids in basic region].

We constructed a phage-displayed random mutation library of Tat38-61(51N/55N), for studying the molecular evolution screening of HIV-1 Tat38-61 epitope. We used primers containing the random nucleotide sequences, and introduced the random mutations at the sites of 51 and 55 amino acids coding sequences into full-length Tat sequences by overlapping PCR. With the randomly mutated full-length Tat as template, the Tat38-61(51N/55N) mutants which contained recognition sequences for the Xba I in both ends were amplified by PCR using the designed primers. The mutants were cloned into Xba I site in the phagemid vector pCANTAB5S, then the recombinants were transformed into E. coli TG1, a phage-displayed the random mutation library of Tat38-61(51N/55N) was constructed by the rescue of help virus M13KO7. The results showed that the library consisted of about 5.0 x 10(6) colonies and the phage library titer was 2.65 x 10(12) TU/mL. More than 56.50% colonies in the library were positive for insertion. Sequence analysis showed that the nucleotides encoding amino acids at the sites of 51 and 55 distributed randomly. The constructed mutation library could meet the requirements for the following molecular evolution screening, and might prepare the Tat mutants for the further study of new Tat vaccine candidates.

[Construction, expression and immunogenicity analysis of a Tat N-terminus-deleted mutant fusion protein of human immunodeficiency virus type 1].

In the study, a gene encoding Tat protein N terminal 1- 21 amino acid residues-deleted mutant (Tat22-101) was amplified by PCR from a full length Tat gene of human immunodeficiency virus type 1, and the prokaryotic expression plasmid pET32a-Tat22-101 was constructed. After identification by digestion with endonucleases and sequencing, the recombinant plasmid pET32a-Tat22-101 was transformed into E. coli BL21(DE3) and expressed with IPTG induction. The mutant fusion protein with deleted Tat N terminal was purified by an affinity chromatography column Ni(2+)-NTA and subsequently identified by SDS-PAGE and Western blotting. The results showed that the molecular weight of the mutant protein was approximately 26.9kD. Furthermore, BALB/c mice were immunized with the mutant protein and the anti-sera were collected. ELISA results showed that the mutant protein preserved its immunogenicity, particularly it could improve the production of antibodies to other epitopes in addition to the N terminal epitope of Tat protein, which might provide some valuable information for the study of Tat functions as well as for development of potential novel HIV Tat vaccine.