Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.707677
Title: Structure and function of the neuraminidase produced by Mannheimia haemolytica
Author: Corona Torres, Ricardo
ISNI:       0000 0004 6063 1955
Awarding Body: University of Birmingham
Current Institution: University of Birmingham
Date of Award: 2017
Availability of Full Text:
Access from EThOS:
Access from Institution:
Abstract:
The Gram negative bacillus Mannheimia haemolytica is a natural inhabitant of the upper respiratory tract in ruminants and the most common secondary agent of the bovine respiratory disease complex. It is known to produce the extracellular neuraminidase NanH, which has a yet unknown biological role but is suspected to be important for bacterial adhesion to host cells, colonisation, capsule synthesis and biofilm formation. The structure of NanH is not known therefore, the functional domains of NanH, the tertiary structure and the residues involved in catalysis were predicted by sequence homology to the coordinates of other neuraminidases solved by crystallography. The catalytic domain was delimited from residues 23 to 435 and purified. The predicted catalytic residues were substituted in the recombinant NanH for confirmation of their role in hydrolysis of sialic acid. The function of the additional domains is unknown but analysis of NanH sequence and other associated genes found in the chromosome of M. haemolytica, suggest the presence of an autotransporter domain. The role of NanH in colonisation and infection is not known however, molecular characterisation is presented in this work. These data provide the basic knowledge required for future studies on using Nanh as a therapeutic and prophylactic target.
Supervisor: Not available Sponsor: Mexican Council for Science & Technology (CONACYT)
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.707677  DOI: Not available
Keywords: QL Zoology ; QR180 Immunology
Share: