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  • 1. Balogun, H. A.
    et al.
    Vasconcelos, N. -M
    Lindberg, Robert
    Södertörns högskola, Institutionen för livsvetenskaper.
    Haeggström, M.
    Moll, K.
    Chen, Q.
    Wahlgren, M.
    Berzins, K.
    Immunogenicity and antigenic properties of Pf332-C231, a fragment of a non-repeat region of the Plasmodium falciparum antigen Pf3322009Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 28, nr 1, s. 90-97Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Antigen Pf332, a megadalton protein has been shown to be associated with the membrane of infected erythrocytes Detailed functional studies on the antigen have remained hampered by the cross-reactive nature of antibodies generated to Pf332 PB32-C231, identified in the C-terminal region of Pf332 was cloned and antibodies against the C231 fragment were shown to react with intact Pf332 antigen by both immunofluorescence and immunoblotting analyses Antibodies to C231 inhibited in vitro Plasmodium falciparum growth efficiently In addition. human sera from malaria-exposed individuals reacted with recombinant C231 We show that Pf332-C231 represents a functional domain and is expected to facilitate further studies on Pf332 as a potential target for protective immune responses and the function of the antigen.

  • 2.
    Buch, Charlotta
    et al.
    Södertörns högskola, Institutionen för livsvetenskaper.
    Lindberg, Robert
    Södertörns högskola, Institutionen för livsvetenskaper.
    Figueroa, Ricardo
    Södertörns högskola, Institutionen för livsvetenskaper.
    Gudise, Santhosh
    Södertörns högskola, Institutionen för livsvetenskaper.
    Onischenko, Evgeny
    Hallberg, Einar
    Södertörns högskola, Institutionen för livsvetenskaper.
    An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells2009Inngår i: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 122, nr 12, s. 2100-2107Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Here, we characterize a transmembrane protein of the nuclear envelope that we name spindle-associated membrane protein 1 (Samp1). The protein is conserved in metazoa and fission yeast and is homologous to Net5 in rat and Ima1 in Schizosaccharomyces pombe. We show that, in human cells, the protein is a membrane-spanning polypeptide with an apparent molecular mass of 43 kDa. This is consistent with a predicted polypeptide of 392 amino acids that has five transmembrane segments and its C-terminus exposed to the nucleoplasm. During interphase, Samp1 was specifically distributed in the inner nuclear membrane. Post-transcriptional silencing of Samp1 expression resulted in separation of centrosomes from the nuclear envelope, indicating that it is functionally connected to the cytoskeleton. At the onset of mitosis, most of the protein dispersed out into the ER, as expected. However, during mitosis, a significant fraction of the protein specifically localized to the polar regions of the mitotic spindle. We demonstrate for the first time, in human cells, the existence of a membranous structure overlapping with the mitotic spindle. Interestingly, another integral inner nuclear membrane protein, emerin, was absent from the spindle-associated membranes. Thus, Samp1 defines a specific membrane domain associated with the mitotic spindle.

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