Nhân một trường hợp bệnh nhân hội chứng thận hư bẩm sinh do nhiễm giang mai bẩm sinh

2018 ◽  
Author(s):  
Nguyễn Thị Kiên ◽  
Nguyễn Thu Hương
Keyword(s):  
L Protein

Ngày nay, tỉ lệ bệnh nhân mắc hội chứng thận hư bẩm sinh thứ phát do giang mai bẩm sinh là rất hiếm gặp trong thực hành lâm sàng. Chúng tôi trình bày ca bệnh nữ 2 tháng tuổi, vào viện trong tình trạng ho, sốt, bụng cổ chướng. Xét nghiệm cho thấy chức năng thận bình thường với Albumin 11,9 g/l; Protein máu 43,6 g/l; Cholesterol:1,64 mmol/l, Protein niệu 2,8g/l; Protein/Creatinin niệu= 10g/mmol, VDRL và TPHA dương tính. Siêu âm bụng có gan lách to, nhiều dịch ổ bụng tự do. Chụng Xquang ngực có hình ảnh viêm phổi. Bệnh nhân được chẩn đoán hội chứng thận hư do nhiễm giang mai bẩm sinh và được điều trị bằng truyền Albumin, lợi tiểu và kháng sinh Penicilin. Trẻ đáp ứng tốt với điều trị, chỉ số hóa sinh máu về bình thường, Protein niệu về bình thường sau điều trị 2 tuần.

scholarly journals Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 613
Author(s):  
Jing Zhang ◽  
Yongxiang Wang ◽  
Shuwen Fu ◽  
Quan Yuan ◽  
Qianru Wang ◽  
...  
Keyword(s):  
Envelope Proteins ◽  
Full Length ◽  
M Protein ◽  
Intracellular Level ◽  
S Protein ◽  
L Protein ◽  
M Proteins ◽  
B Virus ◽  
Subviral Particle ◽  
Genotype A

Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1mer replication construct of genotype A or D, and viral proteins were analyzed from transfected Huh7 cells. Mutating S gene ATG to prevent expression of full-length S protein eliminated M protein, reduced intracellular level of L protein despite its blocked secretion, and generated a truncated S protein through translation initiation from a downstream ATG. Truncated S protein was secretion deficient and could inhibit secretion of L, M, S proteins from wild-type constructs. Providing full-length S protein in trans rescued L protein secretion and increased its intracellular level from mutants of lost S gene ATG. Lost core protein expression reduced all the three envelope proteins. In conclusion, full-length S protein could sustain intracellular and extracellular L and M proteins, while truncated S protein could block subviral particle secretion.

scholarly journals Single amino acid changes in the mumps virus haemagglutinin–neuraminidase and polymerase proteins are associated with neuroattenuation

2009 ◽  
Vol 90 (7) ◽  
pp. 1741-1747 ◽  
Author(s):  
Tahir H. Malik ◽  
Candie Wolbert ◽  
Laura Nerret ◽  
Christian Sauder ◽  
Steven Rubin
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Change ◽  
Mumps Virus ◽  
Site Directed Mutagenesis ◽  
Single Amino Acid ◽  
Supporting Evidence ◽  
L Protein ◽  
Single Amino Acid Change

It has previously been shown that three amino acid changes, one each in the fusion (F; Ala/Thr-91→Thr), haemagglutinin–neuraminidase (HN; Ser-466→Asn) and polymerase (L; Ile-736→Val) proteins, are associated with attenuation of a neurovirulent clinical isolate of mumps virus (88-1961) following serial passage in vitro. Here, using full-length cDNA plasmid clones and site-directed mutagenesis, it was shown that the single amino acid change in the HN protein and to a lesser extent, the change in the L protein, resulted in neuroattenuation, as assessed in rats. The combination of both amino acid changes caused neuroattenuation of the virus to levels previously reported for the clinical isolate following attenuation in vitro. The amino acid change in the F protein, despite having a dramatic effect on protein function in vitro, was previously shown to not be involved in the observed neuroattenuation, highlighting the importance of conducting confirmatory in vivo studies. This report provides additional supporting evidence for the role of the HN protein as a virulence factor and, as far as is known, is the first report to associate an amino acid change in the L protein with mumps virus neuroattenuation.

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