Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv. / Manfield, I. W.; Bernal Giraldo, Adriana Jimena; Møller, I.; McCartney, L.; Riessa, L.; Knox, J. P.; Willats, W. G. T.

In: Plant Science, Vol. 169, No. 6, 2006, p. 1090-0195.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Manfield, IW, Bernal Giraldo, AJ, Møller, I, McCartney, L, Riessa, L, Knox, JP & Willats, WGT 2006, 'Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv', Plant Science, vol. 169, no. 6, pp. 1090-0195. https://doi.org/10.1016/j.plantsci.2005.07.008

APA

Manfield, I. W., Bernal Giraldo, A. J., Møller, I., McCartney, L., Riessa, L., Knox, J. P., & Willats, W. G. T. (2006). Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv. Plant Science, 169(6), 1090-0195. https://doi.org/10.1016/j.plantsci.2005.07.008

Vancouver

Manfield IW, Bernal Giraldo AJ, Møller I, McCartney L, Riessa L, Knox JP et al. Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv. Plant Science. 2006;169(6):1090-0195. https://doi.org/10.1016/j.plantsci.2005.07.008

Author

Manfield, I. W. ; Bernal Giraldo, Adriana Jimena ; Møller, I. ; McCartney, L. ; Riessa, L. ; Knox, J. P. ; Willats, W. G. T. / Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv. In: Plant Science. 2006 ; Vol. 169, No. 6. pp. 1090-0195.

Bibtex

@article{4fca6ea06c3711dcbee902004c4f4f50,
title = "Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv",
abstract = "Antibody phage display is an increasingly important alternative method for the production of monoclonal antibodies (mAbs) and involves the expression of antibody fragments (scFvs) at the surface of bacteriophage particles. We have previously used this technique to generate a phage mAb (PAM1phage) with specificity for the un-esterified regions of the homogalacturonan backbone of pectic polymers. Although phage particles are essential during mAb selection and amplification, their large size results in phage mAbs being poor probes for immunocytochemistry. In order to overcome this and to extend the utility of the PAM1 mAb, we describe here the production of a phage-free, soluble scFv version of the PAM1 mAb (PAM1scFv). Using the new PAM1scFv probe, the occurrence of the HG epitope recognized can now be localized with high resolution within micro-domains of plant cell walls.",
author = "Manfield, {I. W.} and {Bernal Giraldo}, {Adriana Jimena} and I. M{\o}ller and L. McCartney and L. Riessa and Knox, {J. P.} and Willats, {W. G. T.}",
note = "Keywords: Phage display; scFv; Homogalacturonan; Monoclonal antibody; PAM1",
year = "2006",
doi = "10.1016/j.plantsci.2005.07.008",
language = "English",
volume = "169",
pages = "1090--0195",
journal = "Plant Science",
issn = "0168-9452",
publisher = "Elsevier Ireland Ltd",
number = "6",

}

RIS

TY - JOUR

T1 - Re-engineering of the PAM1 phage display monoclonal antibody to produce a soluble, versatile anti-homogalacturonan scFv

AU - Manfield, I. W.

AU - Bernal Giraldo, Adriana Jimena

AU - Møller, I.

AU - McCartney, L.

AU - Riessa, L.

AU - Knox, J. P.

AU - Willats, W. G. T.

N1 - Keywords: Phage display; scFv; Homogalacturonan; Monoclonal antibody; PAM1

PY - 2006

Y1 - 2006

N2 - Antibody phage display is an increasingly important alternative method for the production of monoclonal antibodies (mAbs) and involves the expression of antibody fragments (scFvs) at the surface of bacteriophage particles. We have previously used this technique to generate a phage mAb (PAM1phage) with specificity for the un-esterified regions of the homogalacturonan backbone of pectic polymers. Although phage particles are essential during mAb selection and amplification, their large size results in phage mAbs being poor probes for immunocytochemistry. In order to overcome this and to extend the utility of the PAM1 mAb, we describe here the production of a phage-free, soluble scFv version of the PAM1 mAb (PAM1scFv). Using the new PAM1scFv probe, the occurrence of the HG epitope recognized can now be localized with high resolution within micro-domains of plant cell walls.

AB - Antibody phage display is an increasingly important alternative method for the production of monoclonal antibodies (mAbs) and involves the expression of antibody fragments (scFvs) at the surface of bacteriophage particles. We have previously used this technique to generate a phage mAb (PAM1phage) with specificity for the un-esterified regions of the homogalacturonan backbone of pectic polymers. Although phage particles are essential during mAb selection and amplification, their large size results in phage mAbs being poor probes for immunocytochemistry. In order to overcome this and to extend the utility of the PAM1 mAb, we describe here the production of a phage-free, soluble scFv version of the PAM1 mAb (PAM1scFv). Using the new PAM1scFv probe, the occurrence of the HG epitope recognized can now be localized with high resolution within micro-domains of plant cell walls.

U2 - 10.1016/j.plantsci.2005.07.008

DO - 10.1016/j.plantsci.2005.07.008

M3 - Journal article

VL - 169

SP - 1090

EP - 1195

JO - Plant Science

JF - Plant Science

SN - 0168-9452

IS - 6

ER -

ID: 1100691