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NMR solution structure of a cyanovirin homolog from wheat head blight fungus.

ABSTRACT: Members of the cyanovirin-N homolog (CVNH) lectin family are found in bacteria, fungi and plants. As part of our ongoing work on CVNH structure-function studies, we determined the high-resolution NMR solution structure of the homolog from the wheat head blight disease causing ascomycetous fungus Gibberella zeae (or Fusarium graminearum), hereafter called GzCVNH. Like cyanovirin-N (CV-N), GzCVNH comprises two tandem sequence repeats and the protein sequence exhibits 30% identity with CV-N. The overall structure is similar to those of other members of the CVNH family, with the conserved pseudo-symmetric halves of the structure, domains A and B, closely resembling recently determined structures of Tuber borchii, Neurospora crassa, and Ceratopteris richardii CVNH proteins. Although GzCVNH exhibits a similar glycan recognition profile to CV-N and specifically binds to Man?(1-2)Man?, its weak carbohydrate binding affinity to only one binding site is insufficient for conferring anti-HIV activity.

SUBMITTER: Matei E

PROVIDER: S-EPMC3076533 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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NMR solution structure of a cyanovirin homolog from wheat head blight fungus.

Matei Elena E Louis John M JM Jee JunGoo J Gronenborn Angela M AM

Proteins 20110301 5

Members of the cyanovirin-N homolog (CVNH) lectin family are found in bacteria, fungi and plants. As part of our ongoing work on CVNH structure-function studies, we determined the high-resolution NMR solution structure of the homolog from the wheat head blight disease causing ascomycetous fungus Gibberella zeae (or Fusarium graminearum), hereafter called GzCVNH. Like cyanovirin-N (CV-N), GzCVNH comprises two tandem sequence repeats and the protein sequence exhibits 30% identity with CV-N. The ov ...[more]

PMID: 21365681

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