Back Cover. Issue 5 (1st February 2023)
- Record Type:
- Journal Article
- Title:
- Back Cover. Issue 5 (1st February 2023)
- Main Title:
- Back Cover
- Abstract:
- Abstract : Proteus mirabilis and Proteus vulgaris are zoonotic pathogens which can cause public health disease. Owing to their antibiotic‐resistance, developing vaccines against these pathogens is urgently required. Herein, we describe the first synthesis of the common O‐antigen (trisaccharide to nonasaccharide) of Proteus mirabilis OE and Proteus vulgaris TG 103. Two challenging 1, 2‐ cis ‐glycosidic bonds were successfully constructed by use of conformation‐restrained donors under bifunctional organothiourea catalysis or gold(I) catalysis. A primary immunological evaluation was carried out and the results revealed that the synthetic common O‐antigens both hexasaccharide and nonasaccharide can strongly bind with the IgG antibodies in the sera. More details are discussed in the article by Zhang et al . on page 535—543. Abstract : Proteus mirabilis and Proteus vulgaris are zoonotic pathogens which can cause public health disease. Owing to their antibiotic‐resistance, developing vaccines against these pathogens is urgently required. Herein, we describe the first synthesis of the common O‐antigen (trisaccharide to nonasaccharide) of Proteus mirabilis OE and Proteus vulgaris TG 103. Two challenging 1, 2‐ cis ‐glycosidic bonds were successfully constructed by use of conformation‐restrained donors under bifunctional organothiourea catalysis or gold(I) catalysis. A primary immunological evaluation was carried out and the results revealed that the synthetic common O‐antigens bothAbstract : Proteus mirabilis and Proteus vulgaris are zoonotic pathogens which can cause public health disease. Owing to their antibiotic‐resistance, developing vaccines against these pathogens is urgently required. Herein, we describe the first synthesis of the common O‐antigen (trisaccharide to nonasaccharide) of Proteus mirabilis OE and Proteus vulgaris TG 103. Two challenging 1, 2‐ cis ‐glycosidic bonds were successfully constructed by use of conformation‐restrained donors under bifunctional organothiourea catalysis or gold(I) catalysis. A primary immunological evaluation was carried out and the results revealed that the synthetic common O‐antigens both hexasaccharide and nonasaccharide can strongly bind with the IgG antibodies in the sera. More details are discussed in the article by Zhang et al . on page 535—543. Abstract : Proteus mirabilis and Proteus vulgaris are zoonotic pathogens which can cause public health disease. Owing to their antibiotic‐resistance, developing vaccines against these pathogens is urgently required. Herein, we describe the first synthesis of the common O‐antigen (trisaccharide to nonasaccharide) of Proteus mirabilis OE and Proteus vulgaris TG 103. Two challenging 1, 2‐ cis ‐glycosidic bonds were successfully constructed by use of conformation‐restrained donors under bifunctional organothiourea catalysis or gold(I) catalysis. A primary immunological evaluation was carried out and the results revealed that the synthetic common O‐antigens both hexasaccharide and nonasaccharide can strongly bind with the IgG antibodies in the sera. More details are discussed in the article by Zhang et al . on page 535—543. … (more)
- Is Part Of:
- Chinese journal of chemistry. Volume 41:Issue 5(2023)
- Journal:
- Chinese journal of chemistry
- Issue:
- Volume 41:Issue 5(2023)
- Issue Display:
- Volume 41, Issue 5 (2023)
- Year:
- 2023
- Volume:
- 41
- Issue:
- 5
- Issue Sort Value:
- 2023-0041-0005-0000
- Page Start:
- 620
- Page End:
- 620
- Publication Date:
- 2023-02-01
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1614-7065 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cjoc.202390055 ↗
- Languages:
- English
- ISSNs:
- 1001-604X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3180.299500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 25530.xml