Conservation of fiber structure and CD46 usage by subgroup B2 adenoviruses

Lars Pache; Sangita Venkataraman; Glen R. Nemerow; Vijay S. Reddy

doi:10.1016/j.virol.2008.02.013

Conservation of fiber structure and CD46 usage by subgroup B2 adenoviruses

Lars Pache
, Sangita Venkataraman
, Glen R. Nemerow
, Vijay S. Reddy

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Most subgroup B2 adenoviruses use CD46 as their primary receptor. Recent structural and mutagenesis studies suggested that Ad11 and Ad35 likely engage this receptor in a very similar fashion. However, no comparative studies assessing the cell-associated CD46 binding efficiencies of different Ad fibers have been performed. We solved the crystal structure of Ad35 fiber knob and constructed a model of the fiber knob complexed with CD46. Comparison of our model with that of Ad11-CD46 showed that despite a larger CD46-interacting region in the IJ loop of Ad11, the buried surface area was very similar, suggesting that both fiber knobs might exhibit similar binding. In support of this, cell based competition studies demonstrated almost identical binding efficiencies of Ad11 and Ad35 fibers to cell surface CD46. These findings shed further light on CD46 association by Ad and could impact the selection of novel Ad types for gene transfer.

Original language	English (US)
Pages (from-to)	573-579
Number of pages	7
Journal	Virology
Volume	375
Issue number	2
DOIs	https://doi.org/10.1016/j.virol.2008.02.013
State	Published - Jun 5 2008
Externally published	Yes

Bibliographical note

Funding Information:
We thank Joan Gausepohl and Samia N. Naccache for comments and editorial suggestions. This work was supported by NIH grant R24 EY017540-01, NIH grant R56 AI070771 to V.S.R. and NIH grant RO1 EY11431 to G.R.N. This is done under Manuscript #19298 of The Scripps Research Institute. The coordinates of the Ad35 fiber knob structure have been deposited at RCSB PDB (PDB-ID: 3BQ4).

Keywords

Ad11
Ad35
Adenovirus, CD46
Fiber
Gene therapy
Knob
Membrane cofactor protein
Structure
Vector

Publisher link

10.1016/j.virol.2008.02.013

Find It

Find It at U of M Libraries

Cite this

@article{435d9fd1321f4ff0a140cc5018d845cb,

title = "Conservation of fiber structure and CD46 usage by subgroup B2 adenoviruses",

abstract = "Most subgroup B2 adenoviruses use CD46 as their primary receptor. Recent structural and mutagenesis studies suggested that Ad11 and Ad35 likely engage this receptor in a very similar fashion. However, no comparative studies assessing the cell-associated CD46 binding efficiencies of different Ad fibers have been performed. We solved the crystal structure of Ad35 fiber knob and constructed a model of the fiber knob complexed with CD46. Comparison of our model with that of Ad11-CD46 showed that despite a larger CD46-interacting region in the IJ loop of Ad11, the buried surface area was very similar, suggesting that both fiber knobs might exhibit similar binding. In support of this, cell based competition studies demonstrated almost identical binding efficiencies of Ad11 and Ad35 fibers to cell surface CD46. These findings shed further light on CD46 association by Ad and could impact the selection of novel Ad types for gene transfer.",

keywords = "Ad11, Ad35, Adenovirus, CD46, Fiber, Gene therapy, Knob, Membrane cofactor protein, Structure, Vector",

author = "Lars Pache and Sangita Venkataraman and Nemerow, \{Glen R.\} and Reddy, \{Vijay S.\}",

note = "Funding Information: We thank Joan Gausepohl and Samia N. Naccache for comments and editorial suggestions. This work was supported by NIH grant R24 EY017540-01, NIH grant R56 AI070771 to V.S.R. and NIH grant RO1 EY11431 to G.R.N. This is done under Manuscript \#19298 of The Scripps Research Institute. The coordinates of the Ad35 fiber knob structure have been deposited at RCSB PDB (PDB-ID: 3BQ4).",

year = "2008",

month = jun,

day = "5",

doi = "10.1016/j.virol.2008.02.013",

language = "English (US)",

volume = "375",

pages = "573--579",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Conservation of fiber structure and CD46 usage by subgroup B2 adenoviruses

AU - Pache, Lars

AU - Venkataraman, Sangita

AU - Nemerow, Glen R.

AU - Reddy, Vijay S.

N1 - Funding Information: We thank Joan Gausepohl and Samia N. Naccache for comments and editorial suggestions. This work was supported by NIH grant R24 EY017540-01, NIH grant R56 AI070771 to V.S.R. and NIH grant RO1 EY11431 to G.R.N. This is done under Manuscript #19298 of The Scripps Research Institute. The coordinates of the Ad35 fiber knob structure have been deposited at RCSB PDB (PDB-ID: 3BQ4).

PY - 2008/6/5

Y1 - 2008/6/5

N2 - Most subgroup B2 adenoviruses use CD46 as their primary receptor. Recent structural and mutagenesis studies suggested that Ad11 and Ad35 likely engage this receptor in a very similar fashion. However, no comparative studies assessing the cell-associated CD46 binding efficiencies of different Ad fibers have been performed. We solved the crystal structure of Ad35 fiber knob and constructed a model of the fiber knob complexed with CD46. Comparison of our model with that of Ad11-CD46 showed that despite a larger CD46-interacting region in the IJ loop of Ad11, the buried surface area was very similar, suggesting that both fiber knobs might exhibit similar binding. In support of this, cell based competition studies demonstrated almost identical binding efficiencies of Ad11 and Ad35 fibers to cell surface CD46. These findings shed further light on CD46 association by Ad and could impact the selection of novel Ad types for gene transfer.

AB - Most subgroup B2 adenoviruses use CD46 as their primary receptor. Recent structural and mutagenesis studies suggested that Ad11 and Ad35 likely engage this receptor in a very similar fashion. However, no comparative studies assessing the cell-associated CD46 binding efficiencies of different Ad fibers have been performed. We solved the crystal structure of Ad35 fiber knob and constructed a model of the fiber knob complexed with CD46. Comparison of our model with that of Ad11-CD46 showed that despite a larger CD46-interacting region in the IJ loop of Ad11, the buried surface area was very similar, suggesting that both fiber knobs might exhibit similar binding. In support of this, cell based competition studies demonstrated almost identical binding efficiencies of Ad11 and Ad35 fibers to cell surface CD46. These findings shed further light on CD46 association by Ad and could impact the selection of novel Ad types for gene transfer.

KW - Ad11

KW - Ad35

KW - Adenovirus, CD46

KW - Fiber

KW - Gene therapy

KW - Knob

KW - Membrane cofactor protein

KW - Structure

KW - Vector

UR - https://www.scopus.com/pages/publications/43449111180

UR - https://www.scopus.com/pages/publications/43449111180#tab=citedBy

U2 - 10.1016/j.virol.2008.02.013

DO - 10.1016/j.virol.2008.02.013

M3 - Article

C2 - 18336857

AN - SCOPUS:43449111180

SN - 0042-6822

VL - 375

SP - 573

EP - 579

JO - Virology

JF - Virology

IS - 2

ER -

Conservation of fiber structure and CD46 usage by subgroup B2 adenoviruses

Abstract

Bibliographical note

Keywords

Publisher link

Find It

Other files and links

Fingerprint

Cite this