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Immune and artificial selection in the hemagglutinin (H) glycoprotein of measles virus

Immune and artificial selection in the hemagglutinin (H) glycoprotein of measles virus
Immune and artificial selection in the hemagglutinin (H) glycoprotein of measles virus
We present a maximum likelihood (ML) analysis of the selection pressures that have shaped the evolution of the large (L) protein and the haemagglutinin (H) glycoprotein of measles virus (MV). A number of amino acid sites that have potentially been subject to adaptive evolution were identified in the H protein using sequences from every known genotype of MV. All but one of these putative positively selected sites reside within the ectodomain of the H protein, where they often show an association with positions of potential B-cell epitopes and sites known to interact with the CD46 receptor. This suggests that MV may be under pressure from the immune system, albeit relatively weakly, to alter sites within epitopes and hence evade the humoral immune response. The positive selection identified at amino acid 546 was shown to correlate with the passage history of MV isolates in Vero cells. We reveal that Vero cell passaging has the potential to introduce an artificial signal of adaptive evolution through selection for changes that increase affinity for the CD46 receptor.

0022-1317
2463-2474
Woelk, Christopher H.
4d3af0fd-658f-4626-b3b5-49a6192bcf7d
Jin, Li
fb1eef11-3d16-41c1-b9e5-0ff887270f75
Holmes, Edward C.
0dab0ee7-07f4-429c-a809-e181fde89b0f
Brown, David W.G.
eddae733-23b7-4e47-b3ac-218de6faa92c
Woelk, Christopher H.
4d3af0fd-658f-4626-b3b5-49a6192bcf7d
Jin, Li
fb1eef11-3d16-41c1-b9e5-0ff887270f75
Holmes, Edward C.
0dab0ee7-07f4-429c-a809-e181fde89b0f
Brown, David W.G.
eddae733-23b7-4e47-b3ac-218de6faa92c

Woelk, Christopher H., Jin, Li, Holmes, Edward C. and Brown, David W.G. (2001) Immune and artificial selection in the hemagglutinin (H) glycoprotein of measles virus. Journal of General Virology, 82 (10), 2463-2474. (PMID:11562539)

Record type: Article

Abstract

We present a maximum likelihood (ML) analysis of the selection pressures that have shaped the evolution of the large (L) protein and the haemagglutinin (H) glycoprotein of measles virus (MV). A number of amino acid sites that have potentially been subject to adaptive evolution were identified in the H protein using sequences from every known genotype of MV. All but one of these putative positively selected sites reside within the ectodomain of the H protein, where they often show an association with positions of potential B-cell epitopes and sites known to interact with the CD46 receptor. This suggests that MV may be under pressure from the immune system, albeit relatively weakly, to alter sites within epitopes and hence evade the humoral immune response. The positive selection identified at amino acid 546 was shown to correlate with the passage history of MV isolates in Vero cells. We reveal that Vero cell passaging has the potential to introduce an artificial signal of adaptive evolution through selection for changes that increase affinity for the CD46 receptor.

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More information

Published date: October 2001
Additional Information: Corrigendum. Page 2469, right hand column, line 29. The amino acid substitutions referred to were transposed; the correct version of the text is given below.Low-affinity CD46-binding isolates can be converted to the high-affinity CD46-binding phenotype by a substitution of Tyr instead of Asn at position 481 (Hsu et al., 1998). Likewise, a substitution of Gly instead of Ser at site 546 has been shown to confer both the properties of CD46 binding and haemadsorption to isolates that were previously defective for these traits (Li et al., 1999).
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 352724
URI: https://eprints.soton.ac.uk/id/eprint/352724
ISSN: 0022-1317
PURE UUID: dbf10c6c-5585-4306-8824-8fe1b93288d7

Catalogue record

Date deposited: 10 Jun 2013 13:23
Last modified: 18 Jul 2017 04:12

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Contributors

Author: Li Jin
Author: Edward C. Holmes
Author: David W.G. Brown

University divisions

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