To advance our understanding of the human immunoglobulin V lambda germline gene contribution to normal as well as autoimmune responses, we have isolated and sequenced six germline genes of the V lambda I subgroup. These genes can be divided into three sub-subgroups on the basis of greater than or equal to 93% nucleotide sequence homology and greater than or equal to 88% deduced amino acid sequence similarity. Examination of all cDNA and protein sequences available for expressed V lambda I genes supports the assignment of these three sub-subgroups. Sequence comparisons also suggest that germline gene members of two of these sub-subgroups, I-a and I-b, are preferentially utilized in the expressed V lambda I repertoire. This finding may be at least partially attributable to regulatory sequence abnormalities apparent in two of the other V lambda I germline genes (Humlv101 and Humlv104) which may interfere with their expression.
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http://dx.doi.org/10.1016/0161-5890(92)90034-u | DOI Listing |
Amyloid
December 2024
Boston University Amyloidosis Center, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Background: Each monoclonal antibody light chain associated with AL amyloidosis has a unique sequence. Defining how these sequences drive amyloid deposition could facilitate faster diagnosis and lead to new treatments.
Methods: Light chain sequences are collected in the AL-Base repository.
Pharmaceuticals (Basel)
November 2024
Boston University Amyloidosis Center, Boston University Chobanian & Avedisian School of Medicine, Boston, MA 02118, USA.
Antibody light chains form amyloid fibrils that lead to progressive tissue damage in amyloid light chain (AL) amyloidosis. The properties of each patient's unique light chain appear to determine its propensity to form amyloid. One factor is N-glycosylation, which is more frequent in amyloid-associated light chains than in light chains from the normal immune repertoire.
View Article and Find Full Text PDFbioRxiv
September 2024
Boston University Amyloidosis Center, Boston University Chobanian & Avedisian School of Medicine, Boston University Medical Campus, 72 E. Concord St, Boston, MA 02118, USA.
Background: Each monoclonal antibody light chain associated with AL amyloidosis has a unique sequence. Defining how these sequences lead to amyloid deposition could facilitate faster diagnosis and lead to new treatments.
Methods: Light chain sequences are collected in the Boston University AL-Base repository.
Dev Comp Immunol
November 2024
College of Grassland Agriculture, Northwest A&F University, Yangling, 712100, China. Electronic address:
Mink are susceptible to viruses such as SARS-CoV-2, H1N1 and H9N2, so they are considered a potential animal model for studying human viral infections. Therefore, it is important to study the immune system of mink. Immunoglobulin (Ig) is an important component of humoral immunity and plays an important role in the body's immune defense.
View Article and Find Full Text PDFAnal Chem
April 2024
Department of Chemistry, University of Massachusetts-Amherst, Amherst, Massachusetts 01003, United States.
Vaccine-induced immune thrombotic thrombocytopenia (VITT) is a rare but dangerous side effect of adenoviral-vectored COVID-19 vaccines. VITT had been linked to production of autoantibodies recognizing platelet factor 4 (PF4). Here, we characterize anti-PF4 antibodies obtained from a VITT patient's blood.
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