| First Author | Hayden TA | Year | 2002 |
| Journal | J Immunol | Volume | 169 |
| Issue | 4 | Pages | 1970-7 |
| PubMed ID | 12165522 | Mgi Jnum | J:309878 |
| Mgi Id | MGI:6708563 | Doi | 10.4049/jimmunol.169.4.1970 |
| Citation | Hayden TA, et al. (2002) Detection of functional V(H)81X heavy chains in adult mice with an assessment of complementarity-determining region 3 diversity and capacity to form pre-B cell receptor. J Immunol 169(4):1970-7 |
| abstractText | Recent reports have indicated that up to 50% of all H chain proteins formed cannot associate with the surrogate L chain complex and therefore fail to form a pre-B cell receptor (pBCR), which is required for allelic exclusion and, in most cases, verifies that the H chain can assemble with the L chain to form an Ab molecule. Certain V(H) genes, such as V(H)81X, appear to be particularly prone to encoding for nonpairing (dysfunctional) H chains. It has been suggested that sequence variability at complementarity-determining region 3, especially when increased by the enzyme TdT, often precludes the ability of V(H)81X-using H chains to form pBCR. To determine whether a motif exists that accounts for the ability of H chains to pair with surrogate L chain complex/L chain, we have bred a mouse line in which H chain recombination can only occur on one allele, allowing us to compile a pool of H chains capable of forming Ab molecules in the absence of dysfunctional H chains. Somewhat unexpectedly, we have found V(H)81X H chains capable of Ab formation and cell surface expression in the presence of TdT. Scrutiny of these H chains has revealed that, although highly prone to encode for dysfunctional H chains, sequence variability is not severely limited among functional V(H)81X H chains. We also demonstrate that surface Ig expression is highly indicative of the capacity of a H chain to form pBCR. |
