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Blood, 15 January 2002, Vol. 99, No. 2, pp. 567-575
IMMUNOBIOLOGY
The different process of class switching and somatic
hypermutation; a novel analysis by CD27 naive B
cells
Haruo Nagumo,
Kazunaga Agematsu,
Norimoto Kobayashi,
Koji Shinozaki,
Sho Hokibara,
Hisashi Nagase,
Masaya Takamoto,
Kozo Yasui,
Kazuo Sugane, and
Atsushi Komiyama
From the Shinshu University, Graduate School of
Medicine, Department of Infectious Immunology and Pediatrics,
Matsumoto, Japan.
The relationship between class switch recombination (CSR) and
somatic hypermutation has been unclear. By using human
CD27 naive B cells, we investigated the somatic
hypermutation and producibility of immunoglobulins (Igs) that occur
after CSR. Although neither adult CD27 nor cord blood B
cells, which showed the unmutated Ig V-region genes, produced IgG, IgM,
or IgA in response to conventional stimuli, they produced IgG and IgM
but not IgA in the presence of Staphylococcus aureus Cowan
strain (SAC) + interleukin-2 (IL-2) + IL-10 + anti-CD40 mAb + CD32 transfectants (CD40/CD32T). The naive B cells also produced IgE when combined with IL-4 + CD40/CD32T. In parallel with IgG production, the expression of mature  1 and 2 transcripts was induced from naive B cells by the stimuli. The CD27
expression on human naive B cells was induced remarkably by CD40
signaling or B-cell receptor engagement, but somatic hypermutation
could not be induced. The proliferation and differentiation into plasma cells were induced from naive B cells, whereas most of the plasma cells
displayed very low levels of mutations in Ig V-region genes. CD27 naive B cells expressed activation-induced cytidine
deaminase messenger RNA by the stimuli later than CD27+
memory B cells. Our results demonstrate that CSR, but not noticeable somatic hypermutation, can be induced from CD27 naive B
cells upon B-cell receptor engagement and CD40 signaling in cooperation
with cytokines, suggesting that CSR and somatic hypermutation processes
can occur independently, and the antibodies produced in this in vitro
system are low-affinity antibodies.
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