Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen

Robert Allen, M. E. Kimmeth, M. Wallhermfechtel, V. Vengelen‐Tyler

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A mouse hybridoma has been isolated which secretes a hemagglutinating monoclonal antibody (MoAb) recognizing the N and ‘N’ blood group antigens. This conclusion is based upon the following observations. First, all red cells expressing either N or one of the alleles of Ss (ie, ‘N’ were strongly agglutinated by the MoAb diluted fourfold. The only cells not reactive were of the M+N‐S‐s‐(U‐) and M+N‐S‐s‐(U+) phenotype and cells (J.R. and A.G.) expressing Lepore‐type hybrids of the MN and Ss sialoglycoproteins, which do not express N or ‘N’. Secondly, red cells of the N+S‐s‐(U‐) phenotype were rendered unreactive to MoAb following treatment of the cells with trypsin, which is known to destroy N antigen activity. Conversely, cells expressing S and/or s maintained their reactivity with MoAb following trypsin treatment, which does not cleave ‘N’ from the Ss sialoglycoprotein. When spent culture medium containing MoAb was diluted and tested against a panel of red cells, the antibody titer fell into two distinct categories depending upon the MNSs phenotype of the target. Red cells expressing either homozygous or heterozygous N‐sialoglycoprotein (N‐ SGP) were agglutinated by 128‐fold diluted MoAb. In contrast, a 16‐fold dilution of MoAb was the endpoint for agglutination of cells lacking N‐ SGP, but expressing S and/or s. 1984 AABB

Original languageEnglish
Pages (from-to)136-140
Number of pages5
JournalTransfusion
Volume24
Issue number2
DOIs
StatePublished - 1 Jan 1984

Fingerprint

Blood Group Antigens
Monoclonal Antibodies
Glycophorin
Phenotype
Trypsin
Agglutination
Hybridomas
Culture Media
Alleles
Antigens
Antibodies

Cite this

Allen, Robert ; Kimmeth, M. E. ; Wallhermfechtel, M. ; Vengelen‐Tyler, V. / Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen. In: Transfusion. 1984 ; Vol. 24, No. 2. pp. 136-140.
@article{06e4ecf2ff754565aeafa9cef1df65a2,
title = "Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen",
abstract = "A mouse hybridoma has been isolated which secretes a hemagglutinating monoclonal antibody (MoAb) recognizing the N and ‘N’ blood group antigens. This conclusion is based upon the following observations. First, all red cells expressing either N or one of the alleles of Ss (ie, ‘N’ were strongly agglutinated by the MoAb diluted fourfold. The only cells not reactive were of the M+N‐S‐s‐(U‐) and M+N‐S‐s‐(U+) phenotype and cells (J.R. and A.G.) expressing Lepore‐type hybrids of the MN and Ss sialoglycoproteins, which do not express N or ‘N’. Secondly, red cells of the N+S‐s‐(U‐) phenotype were rendered unreactive to MoAb following treatment of the cells with trypsin, which is known to destroy N antigen activity. Conversely, cells expressing S and/or s maintained their reactivity with MoAb following trypsin treatment, which does not cleave ‘N’ from the Ss sialoglycoprotein. When spent culture medium containing MoAb was diluted and tested against a panel of red cells, the antibody titer fell into two distinct categories depending upon the MNSs phenotype of the target. Red cells expressing either homozygous or heterozygous N‐sialoglycoprotein (N‐ SGP) were agglutinated by 128‐fold diluted MoAb. In contrast, a 16‐fold dilution of MoAb was the endpoint for agglutination of cells lacking N‐ SGP, but expressing S and/or s. 1984 AABB",
author = "Robert Allen and Kimmeth, {M. E.} and M. Wallhermfechtel and V. Vengelen‐Tyler",
year = "1984",
month = "1",
day = "1",
doi = "10.1046/j.1537-2995.1984.24284173344.x",
language = "English",
volume = "24",
pages = "136--140",
journal = "Transfusion",
issn = "0041-1132",
publisher = "Wiley-Blackwell Publishing Ltd",
number = "2",

}

Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen. / Allen, Robert; Kimmeth, M. E.; Wallhermfechtel, M.; Vengelen‐Tyler, V.

In: Transfusion, Vol. 24, No. 2, 01.01.1984, p. 136-140.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen

AU - Allen, Robert

AU - Kimmeth, M. E.

AU - Wallhermfechtel, M.

AU - Vengelen‐Tyler, V.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - A mouse hybridoma has been isolated which secretes a hemagglutinating monoclonal antibody (MoAb) recognizing the N and ‘N’ blood group antigens. This conclusion is based upon the following observations. First, all red cells expressing either N or one of the alleles of Ss (ie, ‘N’ were strongly agglutinated by the MoAb diluted fourfold. The only cells not reactive were of the M+N‐S‐s‐(U‐) and M+N‐S‐s‐(U+) phenotype and cells (J.R. and A.G.) expressing Lepore‐type hybrids of the MN and Ss sialoglycoproteins, which do not express N or ‘N’. Secondly, red cells of the N+S‐s‐(U‐) phenotype were rendered unreactive to MoAb following treatment of the cells with trypsin, which is known to destroy N antigen activity. Conversely, cells expressing S and/or s maintained their reactivity with MoAb following trypsin treatment, which does not cleave ‘N’ from the Ss sialoglycoprotein. When spent culture medium containing MoAb was diluted and tested against a panel of red cells, the antibody titer fell into two distinct categories depending upon the MNSs phenotype of the target. Red cells expressing either homozygous or heterozygous N‐sialoglycoprotein (N‐ SGP) were agglutinated by 128‐fold diluted MoAb. In contrast, a 16‐fold dilution of MoAb was the endpoint for agglutination of cells lacking N‐ SGP, but expressing S and/or s. 1984 AABB

AB - A mouse hybridoma has been isolated which secretes a hemagglutinating monoclonal antibody (MoAb) recognizing the N and ‘N’ blood group antigens. This conclusion is based upon the following observations. First, all red cells expressing either N or one of the alleles of Ss (ie, ‘N’ were strongly agglutinated by the MoAb diluted fourfold. The only cells not reactive were of the M+N‐S‐s‐(U‐) and M+N‐S‐s‐(U+) phenotype and cells (J.R. and A.G.) expressing Lepore‐type hybrids of the MN and Ss sialoglycoproteins, which do not express N or ‘N’. Secondly, red cells of the N+S‐s‐(U‐) phenotype were rendered unreactive to MoAb following treatment of the cells with trypsin, which is known to destroy N antigen activity. Conversely, cells expressing S and/or s maintained their reactivity with MoAb following trypsin treatment, which does not cleave ‘N’ from the Ss sialoglycoprotein. When spent culture medium containing MoAb was diluted and tested against a panel of red cells, the antibody titer fell into two distinct categories depending upon the MNSs phenotype of the target. Red cells expressing either homozygous or heterozygous N‐sialoglycoprotein (N‐ SGP) were agglutinated by 128‐fold diluted MoAb. In contrast, a 16‐fold dilution of MoAb was the endpoint for agglutination of cells lacking N‐ SGP, but expressing S and/or s. 1984 AABB

UR - http://www.scopus.com/inward/record.url?scp=0021244579&partnerID=8YFLogxK

U2 - 10.1046/j.1537-2995.1984.24284173344.x

DO - 10.1046/j.1537-2995.1984.24284173344.x

M3 - Article

C2 - 6710585

AN - SCOPUS:0021244579

VL - 24

SP - 136

EP - 140

JO - Transfusion

JF - Transfusion

SN - 0041-1132

IS - 2

ER -