A Para-Bombay Blood Group Case Associated with a Novel <b><i>FUT1</i></b> Mutation c.361G&#x3e;A

Abstract

&lt;b&gt;&lt;i&gt;Background:&lt;/i&gt;&lt;/b&gt; Here we report a case of para-Bombay phenotype due to a novel mutation &lt;i&gt;FUT1&lt;/i&gt; c.361G&amp;#x3e;A p.(Ala121Thr) and a nonfunctional allele &lt;i&gt;FUT1&lt;/i&gt;*&lt;i&gt;01N.13&lt;/i&gt;(c.881_882delTT) which showed a discrepancy in the routine ABO blood group typing. &lt;b&gt;&lt;i&gt;Materials and Methods:&lt;/i&gt;&lt;/b&gt; The ABO phenotype and the Lewis blood group were typed with serological methods. The ABH antigens in saliva were determined by a hemagglutination inhibition test. The CDS region of &lt;i&gt;ABO, FUT1&lt;/i&gt;and &lt;i&gt;FUT2&lt;/i&gt; were amplified with polymerase chain reaction and then directly sequenced. The novel mutation was confirmed by cloning and sequencing. Three-dimensional (3-D) structural analysis of the mutant and wild-type Fut1 were performed by the Chimera software. &lt;b&gt;&lt;i&gt;Results:&lt;/i&gt;&lt;/b&gt; A, B and H antigens were not detected on the surface of red blood cells (RBCs) by the serological technique, and the B and H blood group substances were detected in the saliva, while the Lewis phenotype was Le(a–b+). Sequencing and cloning analysis showed the presence of a novel &lt;i&gt;FUT1&lt;/i&gt; mutation c.361G&amp;#x3e;A and a nonfunctional allele &lt;i&gt;FUT1&lt;/i&gt;*&lt;i&gt;01N.13&lt;/i&gt;(c.881_882delTT). The ABO genotype was &lt;i&gt;ABO&lt;/i&gt;*&lt;i&gt;B.01/ABO&lt;/i&gt;*&lt;i&gt;O.01.01&lt;/i&gt;. The in silico analysis showed that the mutation p.(Ala121Thr) of &lt;i&gt;FUT1&lt;/i&gt;did not change the 3-D structure of the whole enzyme but caused a certain amplitude of turnover in the loop region where Ala121 was located. &lt;b&gt;&lt;i&gt;Conclusions:&lt;/i&gt;&lt;/b&gt; A novel &lt;i&gt;FUT1&lt;/i&gt; allele (&lt;i&gt;FUT1&lt;/i&gt;*c.361G&amp;#x3e;A) was identified in a Chinese individual with para-Bombay B phenotype. The &lt;i&gt;FUT1&lt;/i&gt;c.361G&amp;#x3e;A mutation may significantly downregulate the expression of H antigens on RBCs by damaging the enzyme conformation.

ABO blood group antigens and differential glycan expression: Perspective on the evolution of common human enzyme deficiencies

“…Blood group AB was not studied, likely because it is much less common than blood groups A, B, and O. Globally, blood group O is thought to be the most prevalent ABO blood type ( Dean, 2005 ; Storry and Olsson, 2009 ). Para-Bombay phenotype (non-functional FUT1 but active FUT2) has an estimated global prevalence of less than 1:1000 ( Dean, 2005 ; Lei et al., 2021 ; Reid and Olsson, 2012 ). Bombay phenotype (non-functional FUT1 and FUT2) affects approximately 1:10,000 individuals in India and 1:100,000 in Europe ( Talukder et al., 2014 ).…”

Genotyping of the rare Para-Bombay blood group in southern Thailand

“…Mutations that inactivate the FUT1 can result in the para-Bombay phenotype where no A, B or H antigen is produced on the RBC. 17 The H blood group system consists of one antigen H that is carried on glycolipids and glycoproteins on the RBC membrane, where the fucosyltransferase product of the FUT1 synthesizes it and on glycoproteins on epithelial cells and in body fluids, where the fucosyltransferase product of the FUT2 synthesizes it. In group O individuals, the H antigen is the terminal antigen.…”

A novel FUT1*c.889C>T allele associated with the para‐Bombay AB phenotype and computational evaluation of the mutation effect

“…[1][2][3][4][5][6][7][8] According to the accumulated public reports, there are two para-Bombay phenotypes. One is an individual who possesses very few A, B, H (ABH) antigens on red blood cells (RBCs), regardless of the presence or the absence of ABH antigens in secretions, 5,[9][10][11] the other involves individual who lacks ABH antigens on RBCs, but possesses them in secretions. [12][13][14] Single nucleotide variant in the FUT1 gene can impact the function of α-(1,2)-fucosyltransferase 1 (α2FucT1), which leads to H antigen (also A/B antigen) deficiency or partial deficiency in RBCs.…”