Biosynthesis of the Escherichia coli K5 capsular polysaccharide.

نویسندگان

  • G Griffiths
  • B Barrett
  • N Cook
  • I S Roberts
چکیده

299-304 47 Payne, G., Virji, M. and Saunden, J. R ( I 996) in Abstracts of the Tenth International Pathogenic Neisseria Conference (Zollinger, W.D., Frasch, C.E. and Deal, C.D., eds.), pp. 393-394, National Institutes of Health, Bethesda, MD 48 Parge, H. E.. Forest, K T.. Hickey, M. 1.. Christensen, D. A,. Getzoff, E. D. and Tainer, J. A. (I 995) Nature (London) 378, 32-38 49 Forest, K T. and Tainer, J. A. ( 1997) Gene 192, 165I69 50 Kraulis, P. J. ( I99 I ) J. Appl. Crystall. 24, 946-950 5 I Nicholls, A., Sharp, K. and Honig, B. ( I 99 I) Proteins I I , 28 1-296

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Expression of E.coli capsular polysaccharide requires the KfiB protein:A Structural based analysis

Abstract Background and objectives: important virulence factor for many invasive bacterial pathogens of humans. Escherichia coli offer a model system to study the mechanisms by which capsular polysaccharides are synthesized and exported onto the cell surface of bacteria. Biosynthesis of the E consists of the repeat structure -4) GlcA- (1, 4)-GlcNAc- (1-, requires the KfiA,...

متن کامل

Overexpression of UDP-glucose dehydrogenase in Escherichia coli results in decreased biosynthesis of K5 polysaccharide.

The Escherichia coli K5 capsular polysaccharide (glycosaminoglycan) chains are composed of the repeated disaccharide structure: -GlcAbeta1,4-GlcNAcalpha1,4-(where GlcA is glucuronic acid and GlcNAc is N-acetyl-D-glucosamine). The GlcA, present in most glycosaminoglycans, is donated from UDP-GlcA, which, in turn, is generated from UDP-glucose by the enzyme UDP-glucose dehydrogenase (UDPGDH). The...

متن کامل

DNA probes for K-antigen (capsule) typing of Escherichia coli.

DNA restriction fragments derived from the polysaccharide biosynthesis regions of cloned Escherichia coli K1, K5, and K12 capsular antigen genes hybridized only with DNA of strains determined by conventional methods to be of the same K serotype. A probe derived from the common transport region hybridized to all encapsulated E. coli strains.

متن کامل

Escherichia coli K5 heparosan fermentation and improvement by genetic engineering.

N-acetyl heparosan is the precursor for the biosynthesis of the important anticoagulant drug heparin. The E. coli K5 capsular heparosan polysaccharide provides a promising precursor for in vitro chemoenzymatic production of bioengineered heparin. This article explores the improvements of heparosan production for bioengineered heparin by fermentation process engineering and genetic engineering.

متن کامل

Biosynthesis of heparin. Use of Escherichia coli K5 capsular polysaccharide as a model substrate in enzymic polymer-modification reactions.

A capsular polysaccharide from Escherichia coli K5 was previously found to have the same structure, [-(4)beta GlcA(1)----(4)alpha GlcNAc(1)-]n, as that of the non-sulphated precursor polysaccharide in heparin biosynthesis [Vann, Schmidt, Jann & Jann (1981) Eur. J. Biochem. 116, 359-364]. The K5 polysaccharide was N-deacetylated (by hydrazinolysis) and N-sulphated, and was then incubated with de...

متن کامل

E. coli K5 fermentation and the preparation of heparosan, a bioengineered heparin precursor.

Heparosan is an acidic polysaccharide natural product, which serves as the critical precursor in heparin biosynthesis and in the chemoenzymatic synthesis of bioengineered heparin. Heparosan is also the capsular polysaccharide of Escherichia coli K5 strain. The current study was focused on the examination of the fermentation of E. coli K5 with the goal of producing heparosan in high yield and vo...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical Society transactions

دوره 27 4  شماره 

صفحات  -

تاریخ انتشار 1999