{"entity": "researcher", "timestamp": "2026-09-25T03:49:14.213Z", "family": "Zandian", "given": "Arash", "initials": "A", "orcid": "0000-0003-1242-0873", "affiliations": ["Affinity Proteomics, SciLifeLab, School of Biotechnology, KTH - Royal Institute of Technology , SE-171 21 Solna, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/c3a3fc4559174f8aac635879355ca608.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/c3a3fc4559174f8aac635879355ca608"}}, "publications": [{"entity": "publication", "iuid": "1e1c884c85e840159431bc0062137517", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1e1c884c85e840159431bc0062137517.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1e1c884c85e840159431bc0062137517"}}, "title": "SURGE complex of Plasmodium falciparum in the rhoptry-neck (SURFIN4.2-RON4-GLURP) contributes to merozoite invasion.", "authors": [{"family": "Quintana", "given": "Maria Del Pilar", "initials": "MDP", "orcid": "0000-0001-6190-3324", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/073482ee6e7341cdb806dbda2ab67c50.json"}}, {"family": "Ch'ng", "given": "Jun-Hong", "initials": "JH"}, {"family": "Zandian", "given": "Arash", "initials": "A", "orcid": "0000-0003-1242-0873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c3a3fc4559174f8aac635879355ca608.json"}}, {"family": "Imam", "given": "Maryam", "initials": "M"}, {"family": "Hultenby", "given": "Kjell", "initials": "K"}, {"family": "Theisen", "given": "Michael", "initials": "M"}, {"family": "Nilsson", "given": "Peter", "initials": "P"}, {"family": "Qundos", "given": "Ulrika", "initials": "U"}, {"family": "Moll", "given": "Kirsten", "initials": "K"}, {"family": "Chan", "given": "Sherwin", "initials": "S", "orcid": "0000-0002-6406-5570", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5fe0163e0f214388b1a6ac83156df0a0.json"}}, {"family": "Wahlgren", "given": "Mats", "initials": "M"}], "type": "journal article", "published": "2018-08-09", "journal": {"title": "PLoS ONE", "issn": "1932-6203", "volume": "13", "issue": "8", "pages": "e0201669", "issn-l": "1932-6203"}, "abstract": "Plasmodium falciparum invasion into red blood cells (RBCs) is a complex process engaging proteins on the merozoite surface and those contained and sequentially released from the apical organelles (micronemes and rhoptries). Fundamental to invasion is the formation of a moving junction (MJ), a region of close apposition of the merozoite and the RBC plasma membranes, through which the merozoite draws itself before settling into a newly formed parasitophorous vacuole (PV). SURFIN4.2 was identified at the surface of the parasitized RBCs (pRBCs) but was also found apically associated with the merozoite. Using antibodies against the N-terminus of the protein we show the presence of SURFIN4.2 in the neck of the rhoptries, its secretion into the PV and shedding into the culture supernatant upon schizont rupture. Using immunoprecipitation followed by mass spectrometry we describe here a novel protein complex we have named SURGE where SURFIN4.2 forms interacts with the rhoptry neck protein 4 (RON4) and the Glutamate Rich Protein (GLURP). The N-terminal cysteine-rich-domain (CRD) of SURFIN4.2 mediates binding to the RBC membrane and its interaction with RON4 suggests its involvement in the contact between the merozoite apex and the RBC at the MJ. Supporting this suggestion, we also found that polyclonal antibodies to the extracellular domain (including the CRD) of SURFIN4.2 partially inhibit merozoite invasion. We propose that the formation of the SURGE complex participates in the establishment of parasite infection within the PV and the RBCs.", "doi": "10.1371/journal.pone.0201669", "pmid": "30092030", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6084945"}, {"db": "pii", "key": "PONE-D-18-10007"}], "notes": [], "created": "2019-01-17T13:58:02.914Z", "modified": "2026-09-23T12:37:33.285Z"}, {"entity": "publication", "iuid": "ce19b2d2e8fd4440bb99076814bb655f", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/ce19b2d2e8fd4440bb99076814bb655f.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/ce19b2d2e8fd4440bb99076814bb655f"}}, "title": "Antibodies in children with malaria to PfEMP1, RIFIN and SURFIN expressed at the Plasmodium falciparum parasitized red blood cell surface.", "authors": [{"family": "Quintana", "given": "Maria Del Pilar", "initials": "MDP"}, {"family": "Ch'ng", "given": "Jun-Hong", "initials": "JH"}, {"family": "Moll", "given": "Kirsten", "initials": "K"}, {"family": "Zandian", "given": "Arash", "initials": "A", "orcid": "0000-0003-1242-0873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c3a3fc4559174f8aac635879355ca608.json"}}, {"family": "Nilsson", "given": "Peter", "initials": "P"}, {"family": "Idris", "given": "Zulkarnain Md", "initials": "ZM"}, {"family": "Saiwaew", "given": "Somporn", "initials": "S"}, {"family": "Qundos", "given": "Ulrika", "initials": "U"}, {"family": "Wahlgren", "given": "Mats", "initials": "M"}], "type": "journal article", "published": "2018-02-19", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "8", "issue": "1", "pages": "3262", "issn-l": "2045-2322"}, "abstract": "Naturally acquired antibodies to proteins expressed on the Plasmodium falciparum parasitized red blood cell (pRBC) surface steer the course of a malaria infection by reducing sequestration and stimulating phagocytosis of pRBC. Here we have studied a selection of proteins representing three different parasite gene families employing a well-characterized parasite with a severe malaria phenotype (FCR3S1.2). The presence of naturally acquired antibodies, impact on rosetting rate, surface reactivity and opsonization for phagocytosis in relation to different blood groups of the ABO system were assessed in a set of sera from children with mild or complicated malaria from an endemic area. We show that the naturally acquired immune responses, developed during malaria natural infection, have limited access to the pRBCs inside a blood group A rosette. The data also indicate that SURFIN4.2 may have a function at the pRBC surface, particularly during rosette formation, this role however needs to be further validated. Our results also indicate epitopes differentially recognized by rosette-disrupting antibodies on a peptide array. Antibodies towards parasite-derived proteins such as PfEMP1, RIFIN and SURFIN in combination with host factors, essentially the ABO blood group of a malaria patient, are suggested to determine the outcome of a malaria infection.", "doi": "10.1038/s41598-018-21026-4", "pmid": "29459776", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5818650"}, {"db": "pii", "key": "10.1038/s41598-018-21026-4"}], "notes": [], "created": "2018-12-05T12:47:51.587Z", "modified": "2026-09-23T11:45:23.395Z"}, {"entity": "publication", "iuid": "da50f2b3cada4439a81cbf09118abca5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/da50f2b3cada4439a81cbf09118abca5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/da50f2b3cada4439a81cbf09118abca5"}}, "title": "Whole-Proteome Peptide Microarrays for Profiling Autoantibody Repertoires within Multiple Sclerosis and Narcolepsy.", "authors": [{"family": "Zandian", "given": "Arash", "initials": "A", "orcid": "0000-0003-1242-0873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c3a3fc4559174f8aac635879355ca608.json"}}, {"family": "Forsstr\u00f6m", "given": "Bj\u00f6rn", "initials": "B"}, {"family": "H\u00e4ggmark-M\u00e5nberg", "given": "Anna", "initials": "A"}, {"family": "Schwenk", "given": "Jochen M", "initials": "JM"}, {"family": "Uhl\u00e9n", "given": "Mathias", "initials": "M"}, {"family": "Nilsson", "given": "Peter", "initials": "P"}, {"family": "Ayoglu", "given": "Burcu", "initials": "B", "orcid": "0000-0001-7843-2960", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4d75c3ce33814d2b961aef643f0d7f0c.json"}}], "type": "journal article", "published": "2017-03-03", "journal": {"title": "J. Proteome Res.", "issn": "1535-3907", "volume": "16", "issue": "3", "pages": "1300-1314", "issn-l": "1535-3893"}, "abstract": "The underlying molecular mechanisms of autoimmune diseases are poorly understood. To unravel the autoimmune processes across diseases, comprehensive and unbiased analyses of proteins targets recognized by the adaptive immune system are needed. Here we present an approach starting from high-density peptide arrays to characterize autoantibody repertoires and to identify new autoantigens. A set of ten plasma and serum samples from subjects with multiple sclerosis, narcolepsy, and without any disease diagnosis were profiled on a peptide array representing the whole proteome, hosting 2.2 million 12-mer peptides with a six amino acid lateral shift. On the basis of the IgG reactivities found on these whole-proteome peptide microarrays, a set of 23 samples was then studied on a targeted array with 174 000 12-mer peptides of single amino acid lateral shift. Finally, verification of IgG reactivities was conducted with a larger sample set (n = 448) using the bead-based peptide microarrays. The presented workflow employed three different peptide microarray formats to discover and resolve the epitopes of human autoantibodies and revealed two potentially new autoantigens: MAP3K7 in multiple sclerosis and NRXN1 in narcolepsy. The presented strategy provides insights into antibody repertoire reactivity at a peptide level and may accelerate the discovery and validation of autoantigens in human diseases.", "doi": "10.1021/acs.jproteome.6b00916", "pmid": "28121444", "labels": [], "xrefs": [], "notes": [], "created": "2018-12-05T10:01:43.520Z", "modified": "2026-09-23T09:14:57.793Z"}]}