Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus

S.A. Hogenhout, F. van der Wilk, M. Verbeek, R.W. Goldbach, J.F.J.M. van den Heuvel

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Abstract

Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid's primary endosymbiotic bacterium (Buchnera sp.). Mutational analysis of GroEL from the primary endosymbiont of Myzus persicae (MpB GroEL) revealed that the amino acids mediating binding of Potato leafroll virus (PLRV; Luteoviridae) are located within residues 9 to 19 and 427 to 457 of the N-terminal and C-terminal regions, respectively, of the discontinuous equatorial domain. Virus overlay assays with a series of overlapping synthetic decameric peptides and their derivatives demonstrated that R13, K15, L17, and R18 of the N-terminal region and R441 and R445 of the C-terminal region of the equatorial domain of GroEL are critical for PLRV binding. Replacement of R441 and R445 by alanine in full-length MpB GroEL and in MpB GroEL deletion mutants reduced but did not abolish PLRV binding. Alanine substitution of either R13 or K15 eliminated the PLRV-binding capacity of the other and those of L17 and R18. In the predicted tertiary structure of GroEL, the determinants mediating virus binding are juxtaposed in the equatorial plain.
Original languageEnglish
Pages (from-to)4541-4548
JournalJournal of Virology
Volume74
Issue number10
Publication statusPublished - 2000

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Buchnera
Luteoviridae
Potato leafroll virus
Aphids
Solanum tuberosum
alanine
Aphidoidea
Viruses
Alanine
viruses
synthetic peptides
Myzus persicae
endosymbionts
binding capacity
Luteovirus
hemolymph
Virus Attachment
Hemolymph
chemical derivatives
mutants

Cite this

Hogenhout, S. A., van der Wilk, F., Verbeek, M., Goldbach, R. W., & van den Heuvel, J. F. J. M. (2000). Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus. Journal of Virology, 74(10), 4541-4548.
Hogenhout, S.A. ; van der Wilk, F. ; Verbeek, M. ; Goldbach, R.W. ; van den Heuvel, J.F.J.M. / Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus. In: Journal of Virology. 2000 ; Vol. 74, No. 10. pp. 4541-4548.
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abstract = "Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid's primary endosymbiotic bacterium (Buchnera sp.). Mutational analysis of GroEL from the primary endosymbiont of Myzus persicae (MpB GroEL) revealed that the amino acids mediating binding of Potato leafroll virus (PLRV; Luteoviridae) are located within residues 9 to 19 and 427 to 457 of the N-terminal and C-terminal regions, respectively, of the discontinuous equatorial domain. Virus overlay assays with a series of overlapping synthetic decameric peptides and their derivatives demonstrated that R13, K15, L17, and R18 of the N-terminal region and R441 and R445 of the C-terminal region of the equatorial domain of GroEL are critical for PLRV binding. Replacement of R441 and R445 by alanine in full-length MpB GroEL and in MpB GroEL deletion mutants reduced but did not abolish PLRV binding. Alanine substitution of either R13 or K15 eliminated the PLRV-binding capacity of the other and those of L17 and R18. In the predicted tertiary structure of GroEL, the determinants mediating virus binding are juxtaposed in the equatorial plain.",
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Hogenhout, SA, van der Wilk, F, Verbeek, M, Goldbach, RW & van den Heuvel, JFJM 2000, 'Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus', Journal of Virology, vol. 74, no. 10, pp. 4541-4548.

Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus. / Hogenhout, S.A.; van der Wilk, F.; Verbeek, M.; Goldbach, R.W.; van den Heuvel, J.F.J.M.

In: Journal of Virology, Vol. 74, No. 10, 2000, p. 4541-4548.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Identifying the determinants in the equatorial domain of Buchnera GroEL implicated in binding Potato Leafroll Virus

AU - Hogenhout, S.A.

AU - van der Wilk, F.

AU - Verbeek, M.

AU - Goldbach, R.W.

AU - van den Heuvel, J.F.J.M.

PY - 2000

Y1 - 2000

N2 - Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid's primary endosymbiotic bacterium (Buchnera sp.). Mutational analysis of GroEL from the primary endosymbiont of Myzus persicae (MpB GroEL) revealed that the amino acids mediating binding of Potato leafroll virus (PLRV; Luteoviridae) are located within residues 9 to 19 and 427 to 457 of the N-terminal and C-terminal regions, respectively, of the discontinuous equatorial domain. Virus overlay assays with a series of overlapping synthetic decameric peptides and their derivatives demonstrated that R13, K15, L17, and R18 of the N-terminal region and R441 and R445 of the C-terminal region of the equatorial domain of GroEL are critical for PLRV binding. Replacement of R441 and R445 by alanine in full-length MpB GroEL and in MpB GroEL deletion mutants reduced but did not abolish PLRV binding. Alanine substitution of either R13 or K15 eliminated the PLRV-binding capacity of the other and those of L17 and R18. In the predicted tertiary structure of GroEL, the determinants mediating virus binding are juxtaposed in the equatorial plain.

AB - Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid's primary endosymbiotic bacterium (Buchnera sp.). Mutational analysis of GroEL from the primary endosymbiont of Myzus persicae (MpB GroEL) revealed that the amino acids mediating binding of Potato leafroll virus (PLRV; Luteoviridae) are located within residues 9 to 19 and 427 to 457 of the N-terminal and C-terminal regions, respectively, of the discontinuous equatorial domain. Virus overlay assays with a series of overlapping synthetic decameric peptides and their derivatives demonstrated that R13, K15, L17, and R18 of the N-terminal region and R441 and R445 of the C-terminal region of the equatorial domain of GroEL are critical for PLRV binding. Replacement of R441 and R445 by alanine in full-length MpB GroEL and in MpB GroEL deletion mutants reduced but did not abolish PLRV binding. Alanine substitution of either R13 or K15 eliminated the PLRV-binding capacity of the other and those of L17 and R18. In the predicted tertiary structure of GroEL, the determinants mediating virus binding are juxtaposed in the equatorial plain.

M3 - Article

VL - 74

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JO - Journal of Virology

JF - Journal of Virology

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