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Selection of Ig µ Heavy Chains by Complementarity-Determining Region 3 Length and Amino Acid Composition¹

Denise A. Martin^*, Harald Bradl, Tara J. Collins^*, Edith Roth, Hans-Martin Jäck^2, and Gillian E. Wu^*,

^* Department of Immunology, University of Toronto, and Ontario Cancer Institute, Toronto, Canada; Division of Molecular Immunology, Department of Internal Medicine III, Nikolaus Fiebiger Center, University of Erlangen-Nürnberg, Erlangen, Germany; and Faculty of Pure and Applied Science, York University, Toronto, Canada

Although it is generally accepted that Ig heavy chains (HC) are selected at the pre-B cell receptor (pre-BCR) checkpoint, the characteristics of a functional HC and the role of pre-BCR assembly in their selection have remained elusive. We determined the characteristics of HCs that successfully passed the pre-BCR checkpoint by examining transcripts harboring V_H81X and J_H4 gene segments from J_H^+/- and 5^-/-mice. V_H81X-J_H4-HC transcripts isolated from cells before or in the absence of pre-BCR assembly had no distinguishing complementarity-determining region 3 traits. In contrast, transcripts isolated subsequent to passage through the pre-BCR checkpoint had distinctive complementarity-determining regions 3 of nine amino acids in length (49%) and a histidine at position 1 (73%). Hence, our data define specific structural requirements for a functional HC, which is instrumental in shaping the diverse B cell repertoire.

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